CAR-1 (Cytokinesis, Apoptosis, RNA-associated) is the C. elegans ortholog of LSM14/Scd6 family proteins. It contains an N-terminal atypical Sm domain that directly binds RNA, central DFDF/FFD/TFG motifs, and a C-terminal RGG box. CAR-1 is a key component of both P-bodies (cytoplasmic mRNA processing bodies) and P granules (germline-specific ribonucleoprotein particles). It forms an RNA-dependent complex with the DEAD-box RNA helicase CGH-1 (DDX6 ortholog) and the Y-box protein CEY-2, functioning in post-transcriptional regulation of maternally loaded mRNAs. CAR-1 is essential for embryonic cytokinesis, where it is required for formation of interzonal microtubule bundles during anaphase. It also regulates physiological germline apoptosis, with car-1 depletion leading to increased germ cell death. The protein localizes dynamically to P granules that concentrate in germline precursors and to smaller cytoplasmic P-body particles present in all cells of early embryos.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
|
GO:0000932
P-body
|
IBA
GO_REF:0000033 |
ACCEPT |
Summary: CAR-1 is a well-established P-body component. Multiple IDA annotations support P-body localization (PMID:16267265, PMID:18515547, PMID:24367695). CAR-1 colocalizes with DCAP-1, the mRNA decapping component, in cytoplasmic foci that are characteristic of P-bodies (PMID:16267265).
Reason: IBA annotation is fully supported by experimental evidence. CAR-1 localizes with the mRNA decapping component DCAP-1 (PMID:16267265) and localizes to germline P bodies (PMID:18515547). P-body localization is central to CAR-1 function.
|
|
GO:0003729
mRNA binding
|
IBA
GO_REF:0000033 |
ACCEPT |
Summary: CAR-1 contains an atypical Sm domain at its N-terminus that directly binds RNA. The Sm domain and RGG box both bind to poly(U)-sepharose beads in vitro (PMID:16247027). The Sm domain is essential for CAR-1 function but not localization.
Reason: IBA annotation is well-supported. CAR-1 is a predicted RNA-binding protein with demonstrated RNA binding activity. The annotation is appropriately specific as CAR-1 functions in mRNA metabolism through P-body and P-granule complexes.
|
|
GO:0033962
P-body assembly
|
IBA
GO_REF:0000033 |
ACCEPT |
Summary: CAR-1 is a core P-body component, but evidence suggests CGH-1 controls CAR-1 localization and P-body/particle formation rather than CAR-1 driving assembly. In cgh-1 mutants, CAR-1 forms aberrant bar-like structures (PMID:16247027, PMID:24367695).
Reason: IBA annotation is reasonable given CAR-1's conserved role as a P-body component. While CGH-1 appears more upstream in controlling particle assembly, CAR-1 is required for proper P-body function and its depletion affects RNP organization.
|
|
GO:0034063
stress granule assembly
|
IBA
GO_REF:0000033 |
KEEP AS NON CORE |
Summary: While CAR-1 is a known component of RNP granules that share features with stress granules, direct evidence for CAR-1 involvement in stress granule assembly in C. elegans is limited. The annotation is based on phylogenetic inference from yeast Scd6 and other orthologs.
Reason: This annotation is derived from phylogenetic inference. In C. elegans, stress granules and P-bodies colocalize and share components (PMID:24367695), but the primary characterized roles of CAR-1 are in P-body/P-granule function, cytokinesis, and apoptosis regulation rather than stress response.
|
|
GO:0003723
RNA binding
|
IEA
GO_REF:0000120 |
ACCEPT |
Summary: IEA annotation is consistent with experimental evidence. CAR-1 contains Sm domain and RGG box that bind RNA. The more specific mRNA binding (GO:0003729) annotation exists via IBA.
Reason: IEA annotation is valid and supported by experimental evidence demonstrating CAR-1 RNA binding via its Sm domain and RGG box (PMID:16247027). The annotation is appropriately general as a parent term to mRNA binding.
|
|
GO:0005634
nucleus
|
IEA
GO_REF:0000044 |
KEEP AS NON CORE |
Summary: UniProt annotation indicates nuclear localization based on PMID:18430416, which identified CAR-1 as a transcriptional regulator that binds the cdc-48.1 promoter. However, the predominant localization of CAR-1 in other studies is cytoplasmic (P-bodies and P-granules).
Reason: Nuclear localization appears to be a minor or context-specific aspect of CAR-1 function. The primary and well-characterized localizations are to cytoplasmic P-bodies and P-granules. The transcriptional regulator function in PMID:18430416 is atypical compared to other CAR-1 studies.
|
|
GO:0005681
spliceosomal complex
|
IEA
GO_REF:0000043 |
REMOVE |
Summary: This annotation is based on UniProt keyword mapping. While CAR-1 contains an Sm domain related to spliceosomal Sm proteins, CAR-1 itself has an atypical Sm domain and functions in P-body/mRNA metabolism rather than splicing.
Reason: This annotation is misleading. CAR-1 contains an atypical Sm domain that is distinct from canonical spliceosomal Sm domains (PMID:16247027). CAR-1 functions in mRNA metabolism and cytokinesis, not pre-mRNA splicing. The sequence divergence within the Sm domain is predicted to confer unique RNA binding properties to this protein family distinct from spliceosomal Sm proteins.
|
|
GO:0005737
cytoplasm
|
IEA
GO_REF:0000117 |
ACCEPT |
Summary: Cytoplasmic localization is well-supported by multiple experimental studies. CAR-1 localizes to cytoplasmic P-bodies and P-granules.
Reason: IEA annotation is correct and redundant with multiple IDA annotations for cytoplasm localization (PMID:16221731, PMID:16267265). CAR-1 is a cytoplasmic protein that localizes to RNP granules.
|
|
GO:0006351
DNA-templated transcription
|
IEA
GO_REF:0000043 |
KEEP AS NON CORE |
Summary: This annotation is based on UniProt keyword mapping from the transcription regulator function described in PMID:18430416. However, CAR-1's primary characterized function is post-transcriptional mRNA regulation.
Reason: While PMID:18430416 provides evidence for CAR-1 involvement in transcriptional regulation of cdc-48.1, this appears to be a secondary or specialized function. The preponderance of evidence supports CAR-1's primary role in post-transcriptional regulation through P-body/P-granule function.
|
|
GO:0006397
mRNA processing
|
IEA
GO_REF:0000043 |
ACCEPT |
Summary: CAR-1 functions in mRNA metabolism through P-bodies, which are sites of mRNA storage and degradation. CAR-1 colocalizes with DCAP-1, the decapping enzyme.
Reason: IEA annotation is appropriate. CAR-1 is involved in post-transcriptional mRNA regulation as a P-body component. It functions with CGH-1 to regulate maternally loaded mRNAs required for cytokinesis (PMID:16247027).
|
|
GO:0008380
RNA splicing
|
IEA
GO_REF:0000043 |
REMOVE |
Summary: This annotation is based on UniProt keyword mapping, likely from the Sm domain. However, CAR-1 has an atypical Sm domain and functions in mRNA metabolism, not pre-mRNA splicing.
Reason: This annotation is incorrect. CAR-1's atypical Sm domain is functionally distinct from canonical spliceosomal Sm proteins. CAR-1 functions in P-body-mediated mRNA regulation and cytokinesis, not RNA splicing. There is no experimental evidence supporting CAR-1 involvement in splicing.
|
|
GO:0035770
ribonucleoprotein granule
|
IDA
PMID:25261697 Translational control of the oogenic program by components o... |
ACCEPT |
Summary: CAR-1 is a component of OMA ribonucleoprotein particles that regulate translation during oogenesis. CAR-1 was identified as an OMA-1-associated protein in affinity purification experiments.
Reason: IDA annotation is well-supported. CAR-1 localizes to multiple types of RNP granules including P-bodies, P-granules, and OMA RNPs. This annotation captures the general RNP granule localization.
Supporting Evidence:
PMID:25261697
Sep 26. Translational control of the oogenic program by components of OMA ribonucleoprotein particles in Caenorhabditis elegans.
|
|
GO:0000979
RNA polymerase II core promoter sequence-specific DNA binding
|
IDA
PMID:18430416 Involvement of HMG-12 and CAR-1 in the cdc-48.1 expression o... |
UNDECIDED |
Summary: PMID:18430416 identified CAR-1 as binding to Element B in the cdc-48.1 promoter using South-Western blotting from embryonic nuclear extracts. However, this is an unusual function for CAR-1 compared to its well-characterized cytoplasmic RNA metabolism functions.
Reason: The annotation is based on South-Western blotting which identifies proteins that bind DNA, but this method may not distinguish direct from indirect binding. This finding has not been replicated and is inconsistent with CAR-1's primary characterization as a cytoplasmic RNA-binding protein. Further evidence would be needed to confirm this atypical function.
Supporting Evidence:
PMID:18430416
2008 Mar 13. Involvement of HMG-12 and CAR-1 in the cdc-48.1 expression of Caenorhabditis elegans.
|
|
GO:0010628
positive regulation of gene expression
|
IMP
PMID:18430416 Involvement of HMG-12 and CAR-1 in the cdc-48.1 expression o... |
KEEP AS NON CORE |
Summary: car-1(RNAi) reduces cdc-48.1 expression, supporting a positive regulatory role. However, this may be indirect through mRNA stabilization rather than transcriptional activation.
Reason: The annotation reflects a phenotypic observation. Given CAR-1's primary role in mRNA metabolism, the effect on gene expression may be at the post-transcriptional level (mRNA stability/translation) rather than transcriptional activation. The term is broad enough to encompass both possibilities.
Supporting Evidence:
PMID:18430416
2008 Mar 13. Involvement of HMG-12 and CAR-1 in the cdc-48.1 expression of Caenorhabditis elegans.
|
|
GO:0005783
endoplasmic reticulum
|
IDA
PMID:16267265 CAR-1, a protein that localizes with the mRNA decapping comp... |
KEEP AS NON CORE |
Summary: PMID:16267265 reports CAR-1 affects ER organization, but the primary localization data in this paper focuses on P-bodies, P-granules, spindle, and pericentriolar material. ER localization may be indirect or context-specific.
Reason: The paper describes organization of the endoplasmic reticulum is aberrant upon CAR-1 depletion, suggesting CAR-1 affects ER organization. However, ER localization is not a primary characterized site for CAR-1. The relationship may be functional rather than direct localization.
Supporting Evidence:
PMID:16267265
Nov 2. CAR-1, a protein that localizes with the mRNA decapping component DCAP-1, is required for cytokinesis and ER organization in Caenorhabditis elegans embryos.
|
|
GO:0072686
mitotic spindle
|
IDA
PMID:16267265 CAR-1, a protein that localizes with the mRNA decapping comp... |
ACCEPT |
Summary: CAR-1 is required for proper anaphase spindle structure. CAR-1 depletion causes failure of interzonal microtubule bundle formation. The localization to spindle may be related to CAR-1's function in regulating mRNAs required for spindle assembly.
Reason: IDA annotation is supported by functional evidence. CAR-1 depletion causes a specific defect in the microtubule cytoskeleton with loss of interzonal microtubule bundles (PMID:16247027). This suggests CAR-1 localizes to or functions at the spindle during cytokinesis.
Supporting Evidence:
PMID:16267265
Nov 2. CAR-1, a protein that localizes with the mRNA decapping component DCAP-1, is required for cytokinesis and ER organization in Caenorhabditis elegans embryos.
|
|
GO:1990023
mitotic spindle midzone
|
IDA
PMID:16267265 CAR-1, a protein that localizes with the mRNA decapping comp... |
ACCEPT |
Summary: CAR-1 is required for spindle midzone formation. In car-1 depleted embryos, the spindle midzone fails to form, even though midzone components are present (PMID:16267265).
Reason: IDA annotation is well-supported. CAR-1 depletion causes failure of interzonal microtubule bundle formation and loss of AIR-2 and ZEN-4 recruitment to the midzone (PMID:16247027). CAR-1 function is essential for midzone assembly.
Supporting Evidence:
PMID:16267265
Nov 2. CAR-1, a protein that localizes with the mRNA decapping component DCAP-1, is required for cytokinesis and ER organization in Caenorhabditis elegans embryos.
|
|
GO:0005515
protein binding
|
IPI
PMID:25261697 Translational control of the oogenic program by components o... |
MODIFY |
Summary: CAR-1 interacts with OMA-1 in the context of OMA ribonucleoprotein particles. CAR-1 also forms complexes with CGH-1 and CEY-2 (PMID:16247027).
Reason: The term protein binding is too vague and uninformative. CAR-1 has specific, characterized protein interactions including CGH-1 (DDX6 homolog), CEY-2, and OMA-1/2. More specific MF terms should be used if available.
Proposed replacements:
mRNA binding
Supporting Evidence:
PMID:25261697
Sep 26. Translational control of the oogenic program by components of OMA ribonucleoprotein particles in Caenorhabditis elegans.
PMID:16247027
A complex containing the Sm protein CAR-1 and the RNA helicase CGH-1 is required for embryonic cytokinesis in Caenorhabditis elegans.
|
|
GO:0000932
P-body
|
IDA
PMID:24367695 PAB-1, a Caenorhabditis elegans poly(A)-binding protein, reg... |
ACCEPT |
Summary: CAR-1 colocalizes with P-body components CGH-1 and PAB-1 in both P-granules and P-bodies in embryos and gonads (PMID:24367695).
Reason: IDA annotation is well-supported by colocalization studies showing CAR-1 with P-body markers in multiple contexts.
Supporting Evidence:
PMID:24367695
eCollection 2013. PAB-1, a Caenorhabditis elegans poly(A)-binding protein, regulates mRNA metabolism in germline by interacting with CGH-1 and CAR-1.
|
|
GO:0043186
P granule
|
IDA
PMID:24367695 PAB-1, a Caenorhabditis elegans poly(A)-binding protein, reg... |
ACCEPT |
Summary: CAR-1 localizes to P granules, the germline-specific RNP particles in C. elegans. P-granule localization is well-documented across multiple studies.
Reason: IDA annotation is well-supported by multiple studies. CAR-1 localizes to P-granules (germ-line specific ribonucleoprotein particles) (PMID:16267265) and colocalizes with PGL-1, a P-granule marker.
Supporting Evidence:
PMID:24367695
eCollection 2013. PAB-1, a Caenorhabditis elegans poly(A)-binding protein, regulates mRNA metabolism in germline by interacting with CGH-1 and CAR-1.
|
|
GO:1990904
ribonucleoprotein complex
|
IDA
PMID:16247027 A complex containing the Sm protein CAR-1 and the RNA helica... |
ACCEPT |
Summary: CAR-1 is part of a multiprotein RNP complex containing CGH-1 and CEY-2. The interaction with CGH-1 is RNA-dependent.
Reason: IDA annotation is well-supported. CAR-1 is a component of a multiprotein complex that also contains the DEAD box RNA helicase, CGH-1, and a Y-box-containing protein, CEY-2 (PMID:16247027).
Supporting Evidence:
PMID:16247027
A complex containing the Sm protein CAR-1 and the RNA helicase CGH-1 is required for embryonic cytokinesis in Caenorhabditis elegans.
|
|
GO:0000932
P-body
|
IDA
PMID:18515547 C. elegans La-related protein, LARP-1, localizes to germline... |
ACCEPT |
Summary: CAR-1 colocalizes with LARP-1 in germline P-bodies. This study provides additional evidence for CAR-1 P-body localization.
Reason: IDA annotation is supported. LARP-1 colocalizes with P bodies and CAR-1 is established as a P-body component.
Supporting Evidence:
PMID:18515547
C. elegans La-related protein, LARP-1, localizes to germline P bodies and attenuates Ras-MAPK signaling during oogenesis.
|
|
GO:0000242
pericentriolar material
|
IDA
PMID:16267265 CAR-1, a protein that localizes with the mRNA decapping comp... |
ACCEPT |
Summary: CAR-1 localizes to pericentriolar material as shown in PMID:16267265. This localization is consistent with CAR-1's role in spindle-related processes during cytokinesis.
Reason: IDA annotation captures a specific localization relevant to CAR-1's function in cytokinesis and spindle organization.
Supporting Evidence:
PMID:16267265
Nov 2. CAR-1, a protein that localizes with the mRNA decapping component DCAP-1, is required for cytokinesis and ER organization in Caenorhabditis elegans embryos.
|
|
GO:0000932
P-body
|
IDA
PMID:16267265 CAR-1, a protein that localizes with the mRNA decapping comp... |
ACCEPT |
Summary: Original characterization of CAR-1 P-body localization. CAR-1 colocalizes with DCAP-1, the mRNA decapping component, in cytoplasmic foci.
Reason: IDA annotation from the foundational CAR-1 characterization paper. This study established CAR-1 as a P-body component.
Supporting Evidence:
PMID:16267265
Nov 2. CAR-1, a protein that localizes with the mRNA decapping component DCAP-1, is required for cytokinesis and ER organization in Caenorhabditis elegans embryos.
|
|
GO:0005737
cytoplasm
|
IDA
PMID:16221731 A conserved RNA-protein complex component involved in physio... |
ACCEPT |
Summary: CAR-1 localizes to cytoplasmic particles in the gonad and early embryo.
Reason: IDA annotation is well-supported. CAR-1 is primarily a cytoplasmic protein that localizes to various RNP granules.
Supporting Evidence:
PMID:16221731
A conserved RNA-protein complex component involved in physiological germline apoptosis regulation in C.
|
|
GO:0005737
cytoplasm
|
IDA
PMID:16267265 CAR-1, a protein that localizes with the mRNA decapping comp... |
ACCEPT |
Summary: CAR-1 localizes to cytoplasmic foci and P-granules.
Reason: IDA annotation is correct. CAR-1 is a cytoplasmic protein.
Supporting Evidence:
PMID:16267265
Nov 2. CAR-1, a protein that localizes with the mRNA decapping component DCAP-1, is required for cytokinesis and ER organization in Caenorhabditis elegans embryos.
|
|
GO:0043186
P granule
|
IDA
PMID:16221731 A conserved RNA-protein complex component involved in physio... |
ACCEPT |
Summary: CAR-1 localizes to P granules and associates with CGH-1 in a conserved germline RNP complex.
Reason: IDA annotation is well-supported. P-granule localization is a core aspect of CAR-1 function in the germline.
Supporting Evidence:
PMID:16221731
A conserved RNA-protein complex component involved in physiological germline apoptosis regulation in C.
|
|
GO:0043186
P granule
|
IDA
PMID:16247027 A complex containing the Sm protein CAR-1 and the RNA helica... |
ACCEPT |
Summary: CAR-1 localizes to P-granules that concentrate in germline precursors. P-granule localization is confirmed by colocalization with PGL-1.
Reason: IDA annotation is well-supported. CAR-1 localizes to RNA-containing P-granules that concentrate in the germline precursors (PMID:16247027).
Supporting Evidence:
PMID:16247027
A complex containing the Sm protein CAR-1 and the RNA helicase CGH-1 is required for embryonic cytokinesis in Caenorhabditis elegans.
|
|
GO:0043186
P granule
|
IDA
PMID:16267265 CAR-1, a protein that localizes with the mRNA decapping comp... |
ACCEPT |
Summary: Original characterization showing CAR-1 localization to P-granules.
Reason: IDA annotation from foundational CAR-1 paper. P-granule localization is central to CAR-1 germline function.
Supporting Evidence:
PMID:16267265
Nov 2. CAR-1, a protein that localizes with the mRNA decapping component DCAP-1, is required for cytokinesis and ER organization in Caenorhabditis elegans embryos.
|
|
GO:0000281
mitotic cytokinesis
|
IMP
PMID:16247027 A complex containing the Sm protein CAR-1 and the RNA helica... |
NEW |
Summary: CAR-1 is essential for embryonic cytokinesis. car-1(RNAi) and car-1 mutant embryos fail to complete cytokinesis, with cleavage furrows regressing and spindle midzone failing to form.
Reason: This is a core function of CAR-1 not explicitly annotated. CAR-1 was named for Cytokinesis, Apoptosis, RNA-associated reflecting its essential role in cytokinesis. Multiple studies demonstrate cytokinesis failure upon CAR-1 depletion.
Supporting Evidence:
PMID:16247027
A complex containing the Sm protein CAR-1 and the RNA helicase CGH-1 is required for embryonic cytokinesis in Caenorhabditis elegans.
|
|
GO:0017148
negative regulation of translation
|
IBA
GO_REF:0000033 |
NEW |
Summary: CAR-1 functions in translational repression as part of P-body and OMA RNP complexes. CAR-1 is part of the IFET-1/CGH-1/CAR-1/PATR-1 repressive complex.
Reason: This is a core molecular function of CAR-1 based on phylogenetic conservation and its role in P-body-mediated mRNA regulation. CAR-1 associates with translational repressors in OMA RNPs (PMID:25261697).
|
|
GO:0043066
negative regulation of apoptotic process
|
IMP
PMID:16221731 A conserved RNA-protein complex component involved in physio... |
NEW |
Summary: CAR-1 regulates physiological germline apoptosis. car-1(RNAi) leads to increased germline cell death, indicating CAR-1 normally suppresses apoptosis.
Reason: This is a core function of CAR-1 (the A in CAR-1 stands for Apoptosis). Depletion of CAR-1 increases physiological germline apoptosis, demonstrating a negative regulatory role.
Supporting Evidence:
PMID:16221731
A conserved RNA-protein complex component involved in physiological germline apoptosis regulation in C.
|
Q: Is CAR-1's role in transcriptional regulation of cdc-48.1 (PMID:18430416) a true transcriptional function or an indirect effect through mRNA regulation?
Q: What specific mRNAs does CAR-1 regulate to control cytokinesis and anaphase spindle structure?
Q: Does CAR-1 play a direct role in piRNA silencing pathways as suggested by some studies of CAR-1/CGH-1 function?
Experiment: CLIP-seq or RIP-seq to identify direct CAR-1 mRNA targets in embryos and germline.
Experiment: Determine whether CAR-1's effect on cdc-48.1 expression is at the transcriptional or post-transcriptional level.
Experiment: Characterize the specific mRNAs regulated by CAR-1 that are required for interzonal microtubule bundle formation.
id: Q9XW17
gene_symbol: car-1
product_type: PROTEIN
status: COMPLETE
taxon:
id: NCBITaxon:6239
label: Caenorhabditis elegans
description: CAR-1 (Cytokinesis, Apoptosis, RNA-associated) is the C. elegans
ortholog of LSM14/Scd6 family proteins. It contains an N-terminal atypical Sm
domain that directly binds RNA, central DFDF/FFD/TFG motifs, and a C-terminal
RGG box. CAR-1 is a key component of both P-bodies (cytoplasmic mRNA
processing bodies) and P granules (germline-specific ribonucleoprotein
particles). It forms an RNA-dependent complex with the DEAD-box RNA helicase
CGH-1 (DDX6 ortholog) and the Y-box protein CEY-2, functioning in
post-transcriptional regulation of maternally loaded mRNAs. CAR-1 is essential
for embryonic cytokinesis, where it is required for formation of interzonal
microtubule bundles during anaphase. It also regulates physiological germline
apoptosis, with car-1 depletion leading to increased germ cell death. The
protein localizes dynamically to P granules that concentrate in germline
precursors and to smaller cytoplasmic P-body particles present in all cells of
early embryos.
existing_annotations:
- term:
id: GO:0000932
label: P-body
evidence_type: IBA
original_reference_id: GO_REF:0000033
review:
summary: CAR-1 is a well-established P-body component. Multiple IDA
annotations support P-body localization (PMID:16267265, PMID:18515547,
PMID:24367695). CAR-1 colocalizes with DCAP-1, the mRNA decapping
component, in cytoplasmic foci that are characteristic of P-bodies
(PMID:16267265).
action: ACCEPT
reason: IBA annotation is fully supported by experimental evidence. CAR-1
localizes with the mRNA decapping component DCAP-1 (PMID:16267265) and
localizes to germline P bodies (PMID:18515547). P-body localization is
central to CAR-1 function.
- term:
id: GO:0003729
label: mRNA binding
evidence_type: IBA
original_reference_id: GO_REF:0000033
review:
summary: CAR-1 contains an atypical Sm domain at its N-terminus that
directly binds RNA. The Sm domain and RGG box both bind to
poly(U)-sepharose beads in vitro (PMID:16247027). The Sm domain is
essential for CAR-1 function but not localization.
action: ACCEPT
reason: IBA annotation is well-supported. CAR-1 is a predicted RNA-binding
protein with demonstrated RNA binding activity. The annotation is
appropriately specific as CAR-1 functions in mRNA metabolism through
P-body and P-granule complexes.
- term:
id: GO:0033962
label: P-body assembly
evidence_type: IBA
original_reference_id: GO_REF:0000033
review:
summary: CAR-1 is a core P-body component, but evidence suggests CGH-1
controls CAR-1 localization and P-body/particle formation rather than
CAR-1 driving assembly. In cgh-1 mutants, CAR-1 forms aberrant bar-like
structures (PMID:16247027, PMID:24367695).
action: ACCEPT
reason: IBA annotation is reasonable given CAR-1's conserved role as a
P-body component. While CGH-1 appears more upstream in controlling
particle assembly, CAR-1 is required for proper P-body function and its
depletion affects RNP organization.
- term:
id: GO:0034063
label: stress granule assembly
evidence_type: IBA
original_reference_id: GO_REF:0000033
review:
summary: While CAR-1 is a known component of RNP granules that share
features with stress granules, direct evidence for CAR-1 involvement in
stress granule assembly in C. elegans is limited. The annotation is
based on phylogenetic inference from yeast Scd6 and other orthologs.
action: KEEP_AS_NON_CORE
reason: This annotation is derived from phylogenetic inference. In C.
elegans, stress granules and P-bodies colocalize and share components
(PMID:24367695), but the primary characterized roles of CAR-1 are in
P-body/P-granule function, cytokinesis, and apoptosis regulation rather
than stress response.
- term:
id: GO:0003723
label: RNA binding
evidence_type: IEA
original_reference_id: GO_REF:0000120
review:
summary: IEA annotation is consistent with experimental evidence. CAR-1
contains Sm domain and RGG box that bind RNA. The more specific mRNA
binding (GO:0003729) annotation exists via IBA.
action: ACCEPT
reason: IEA annotation is valid and supported by experimental evidence
demonstrating CAR-1 RNA binding via its Sm domain and RGG box
(PMID:16247027). The annotation is appropriately general as a parent
term to mRNA binding.
- term:
id: GO:0005634
label: nucleus
evidence_type: IEA
original_reference_id: GO_REF:0000044
review:
summary: UniProt annotation indicates nuclear localization based on
PMID:18430416, which identified CAR-1 as a transcriptional regulator
that binds the cdc-48.1 promoter. However, the predominant localization
of CAR-1 in other studies is cytoplasmic (P-bodies and P-granules).
action: KEEP_AS_NON_CORE
reason: Nuclear localization appears to be a minor or context-specific
aspect of CAR-1 function. The primary and well-characterized
localizations are to cytoplasmic P-bodies and P-granules. The
transcriptional regulator function in PMID:18430416 is atypical compared
to other CAR-1 studies.
- term:
id: GO:0005681
label: spliceosomal complex
evidence_type: IEA
original_reference_id: GO_REF:0000043
review:
summary: This annotation is based on UniProt keyword mapping. While CAR-1
contains an Sm domain related to spliceosomal Sm proteins, CAR-1 itself
has an atypical Sm domain and functions in P-body/mRNA metabolism rather
than splicing.
action: REMOVE
reason: This annotation is misleading. CAR-1 contains an atypical Sm
domain that is distinct from canonical spliceosomal Sm domains
(PMID:16247027). CAR-1 functions in mRNA metabolism and cytokinesis, not
pre-mRNA splicing. The sequence divergence within the Sm domain is
predicted to confer unique RNA binding properties to this protein family
distinct from spliceosomal Sm proteins.
- term:
id: GO:0005737
label: cytoplasm
evidence_type: IEA
original_reference_id: GO_REF:0000117
review:
summary: Cytoplasmic localization is well-supported by multiple
experimental studies. CAR-1 localizes to cytoplasmic P-bodies and
P-granules.
action: ACCEPT
reason: IEA annotation is correct and redundant with multiple IDA
annotations for cytoplasm localization (PMID:16221731, PMID:16267265).
CAR-1 is a cytoplasmic protein that localizes to RNP granules.
- term:
id: GO:0006351
label: DNA-templated transcription
evidence_type: IEA
original_reference_id: GO_REF:0000043
review:
summary: This annotation is based on UniProt keyword mapping from the
transcription regulator function described in PMID:18430416. However,
CAR-1's primary characterized function is post-transcriptional mRNA
regulation.
action: KEEP_AS_NON_CORE
reason: While PMID:18430416 provides evidence for CAR-1 involvement in
transcriptional regulation of cdc-48.1, this appears to be a secondary
or specialized function. The preponderance of evidence supports CAR-1's
primary role in post-transcriptional regulation through P-body/P-granule
function.
- term:
id: GO:0006397
label: mRNA processing
evidence_type: IEA
original_reference_id: GO_REF:0000043
review:
summary: CAR-1 functions in mRNA metabolism through P-bodies, which are
sites of mRNA storage and degradation. CAR-1 colocalizes with DCAP-1,
the decapping enzyme.
action: ACCEPT
reason: IEA annotation is appropriate. CAR-1 is involved in
post-transcriptional mRNA regulation as a P-body component. It functions
with CGH-1 to regulate maternally loaded mRNAs required for cytokinesis
(PMID:16247027).
- term:
id: GO:0008380
label: RNA splicing
evidence_type: IEA
original_reference_id: GO_REF:0000043
review:
summary: This annotation is based on UniProt keyword mapping, likely from
the Sm domain. However, CAR-1 has an atypical Sm domain and functions in
mRNA metabolism, not pre-mRNA splicing.
action: REMOVE
reason: This annotation is incorrect. CAR-1's atypical Sm domain is
functionally distinct from canonical spliceosomal Sm proteins. CAR-1
functions in P-body-mediated mRNA regulation and cytokinesis, not RNA
splicing. There is no experimental evidence supporting CAR-1 involvement
in splicing.
- term:
id: GO:0035770
label: ribonucleoprotein granule
evidence_type: IDA
original_reference_id: PMID:25261697
review:
summary: CAR-1 is a component of OMA ribonucleoprotein particles that
regulate translation during oogenesis. CAR-1 was identified as an
OMA-1-associated protein in affinity purification experiments.
action: ACCEPT
reason: IDA annotation is well-supported. CAR-1 localizes to multiple
types of RNP granules including P-bodies, P-granules, and OMA RNPs. This
annotation captures the general RNP granule localization.
supported_by:
- reference_id: PMID:25261697
supporting_text: Sep 26. Translational control of the oogenic program
by components of OMA ribonucleoprotein particles in Caenorhabditis
elegans.
- term:
id: GO:0000979
label: RNA polymerase II core promoter sequence-specific DNA binding
evidence_type: IDA
original_reference_id: PMID:18430416
review:
summary: PMID:18430416 identified CAR-1 as binding to Element B in the
cdc-48.1 promoter using South-Western blotting from embryonic nuclear
extracts. However, this is an unusual function for CAR-1 compared to its
well-characterized cytoplasmic RNA metabolism functions.
action: UNDECIDED
reason: The annotation is based on South-Western blotting which identifies
proteins that bind DNA, but this method may not distinguish direct from
indirect binding. This finding has not been replicated and is
inconsistent with CAR-1's primary characterization as a cytoplasmic
RNA-binding protein. Further evidence would be needed to confirm this
atypical function.
supported_by:
- reference_id: PMID:18430416
supporting_text: 2008 Mar 13. Involvement of HMG-12 and CAR-1 in the
cdc-48.1 expression of Caenorhabditis elegans.
- term:
id: GO:0010628
label: positive regulation of gene expression
evidence_type: IMP
original_reference_id: PMID:18430416
review:
summary: car-1(RNAi) reduces cdc-48.1 expression, supporting a positive
regulatory role. However, this may be indirect through mRNA
stabilization rather than transcriptional activation.
action: KEEP_AS_NON_CORE
reason: The annotation reflects a phenotypic observation. Given CAR-1's
primary role in mRNA metabolism, the effect on gene expression may be at
the post-transcriptional level (mRNA stability/translation) rather than
transcriptional activation. The term is broad enough to encompass both
possibilities.
supported_by:
- reference_id: PMID:18430416
supporting_text: 2008 Mar 13. Involvement of HMG-12 and CAR-1 in the
cdc-48.1 expression of Caenorhabditis elegans.
- term:
id: GO:0005783
label: endoplasmic reticulum
evidence_type: IDA
original_reference_id: PMID:16267265
review:
summary: PMID:16267265 reports CAR-1 affects ER organization, but the
primary localization data in this paper focuses on P-bodies, P-granules,
spindle, and pericentriolar material. ER localization may be indirect or
context-specific.
action: KEEP_AS_NON_CORE
reason: The paper describes organization of the endoplasmic reticulum is
aberrant upon CAR-1 depletion, suggesting CAR-1 affects ER organization.
However, ER localization is not a primary characterized site for CAR-1.
The relationship may be functional rather than direct localization.
supported_by:
- reference_id: PMID:16267265
supporting_text: Nov 2. CAR-1, a protein that localizes with the mRNA
decapping component DCAP-1, is required for cytokinesis and ER
organization in Caenorhabditis elegans embryos.
- term:
id: GO:0072686
label: mitotic spindle
evidence_type: IDA
original_reference_id: PMID:16267265
review:
summary: CAR-1 is required for proper anaphase spindle structure. CAR-1
depletion causes failure of interzonal microtubule bundle formation. The
localization to spindle may be related to CAR-1's function in regulating
mRNAs required for spindle assembly.
action: ACCEPT
reason: IDA annotation is supported by functional evidence. CAR-1
depletion causes a specific defect in the microtubule cytoskeleton with
loss of interzonal microtubule bundles (PMID:16247027). This suggests
CAR-1 localizes to or functions at the spindle during cytokinesis.
supported_by:
- reference_id: PMID:16267265
supporting_text: Nov 2. CAR-1, a protein that localizes with the mRNA
decapping component DCAP-1, is required for cytokinesis and ER
organization in Caenorhabditis elegans embryos.
- term:
id: GO:1990023
label: mitotic spindle midzone
evidence_type: IDA
original_reference_id: PMID:16267265
review:
summary: CAR-1 is required for spindle midzone formation. In car-1
depleted embryos, the spindle midzone fails to form, even though midzone
components are present (PMID:16267265).
action: ACCEPT
reason: IDA annotation is well-supported. CAR-1 depletion causes failure
of interzonal microtubule bundle formation and loss of AIR-2 and ZEN-4
recruitment to the midzone (PMID:16247027). CAR-1 function is essential
for midzone assembly.
supported_by:
- reference_id: PMID:16267265
supporting_text: Nov 2. CAR-1, a protein that localizes with the mRNA
decapping component DCAP-1, is required for cytokinesis and ER
organization in Caenorhabditis elegans embryos.
- term:
id: GO:0005515
label: protein binding
evidence_type: IPI
original_reference_id: PMID:25261697
review:
summary: CAR-1 interacts with OMA-1 in the context of OMA
ribonucleoprotein particles. CAR-1 also forms complexes with CGH-1 and
CEY-2 (PMID:16247027).
action: MODIFY
reason: The term protein binding is too vague and uninformative. CAR-1 has
specific, characterized protein interactions including CGH-1 (DDX6
homolog), CEY-2, and OMA-1/2. More specific MF terms should be used if
available.
proposed_replacement_terms:
- id: GO:0003729
label: mRNA binding
additional_reference_ids:
- PMID:16247027
supported_by:
- reference_id: PMID:25261697
supporting_text: Sep 26. Translational control of the oogenic program
by components of OMA ribonucleoprotein particles in Caenorhabditis
elegans.
- reference_id: PMID:16247027
supporting_text: A complex containing the Sm protein CAR-1 and the RNA
helicase CGH-1 is required for embryonic cytokinesis in
Caenorhabditis elegans.
- term:
id: GO:0000932
label: P-body
evidence_type: IDA
original_reference_id: PMID:24367695
review:
summary: CAR-1 colocalizes with P-body components CGH-1 and PAB-1 in both
P-granules and P-bodies in embryos and gonads (PMID:24367695).
action: ACCEPT
reason: IDA annotation is well-supported by colocalization studies showing
CAR-1 with P-body markers in multiple contexts.
supported_by:
- reference_id: PMID:24367695
supporting_text: eCollection 2013. PAB-1, a Caenorhabditis elegans
poly(A)-binding protein, regulates mRNA metabolism in germline by
interacting with CGH-1 and CAR-1.
- term:
id: GO:0043186
label: P granule
evidence_type: IDA
original_reference_id: PMID:24367695
review:
summary: CAR-1 localizes to P granules, the germline-specific RNP
particles in C. elegans. P-granule localization is well-documented
across multiple studies.
action: ACCEPT
reason: IDA annotation is well-supported by multiple studies. CAR-1
localizes to P-granules (germ-line specific ribonucleoprotein particles)
(PMID:16267265) and colocalizes with PGL-1, a P-granule marker.
supported_by:
- reference_id: PMID:24367695
supporting_text: eCollection 2013. PAB-1, a Caenorhabditis elegans
poly(A)-binding protein, regulates mRNA metabolism in germline by
interacting with CGH-1 and CAR-1.
- term:
id: GO:1990904
label: ribonucleoprotein complex
evidence_type: IDA
original_reference_id: PMID:16247027
review:
summary: CAR-1 is part of a multiprotein RNP complex containing CGH-1 and
CEY-2. The interaction with CGH-1 is RNA-dependent.
action: ACCEPT
reason: IDA annotation is well-supported. CAR-1 is a component of a
multiprotein complex that also contains the DEAD box RNA helicase,
CGH-1, and a Y-box-containing protein, CEY-2 (PMID:16247027).
supported_by:
- reference_id: PMID:16247027
supporting_text: A complex containing the Sm protein CAR-1 and the RNA
helicase CGH-1 is required for embryonic cytokinesis in
Caenorhabditis elegans.
- term:
id: GO:0000932
label: P-body
evidence_type: IDA
original_reference_id: PMID:18515547
review:
summary: CAR-1 colocalizes with LARP-1 in germline P-bodies. This study
provides additional evidence for CAR-1 P-body localization.
action: ACCEPT
reason: IDA annotation is supported. LARP-1 colocalizes with P bodies and
CAR-1 is established as a P-body component.
supported_by:
- reference_id: PMID:18515547
supporting_text: C. elegans La-related protein, LARP-1, localizes to
germline P bodies and attenuates Ras-MAPK signaling during
oogenesis.
- term:
id: GO:0000242
label: pericentriolar material
evidence_type: IDA
original_reference_id: PMID:16267265
review:
summary: CAR-1 localizes to pericentriolar material as shown in
PMID:16267265. This localization is consistent with CAR-1's role in
spindle-related processes during cytokinesis.
action: ACCEPT
reason: IDA annotation captures a specific localization relevant to
CAR-1's function in cytokinesis and spindle organization.
supported_by:
- reference_id: PMID:16267265
supporting_text: Nov 2. CAR-1, a protein that localizes with the mRNA
decapping component DCAP-1, is required for cytokinesis and ER
organization in Caenorhabditis elegans embryos.
- term:
id: GO:0000932
label: P-body
evidence_type: IDA
original_reference_id: PMID:16267265
review:
summary: Original characterization of CAR-1 P-body localization. CAR-1
colocalizes with DCAP-1, the mRNA decapping component, in cytoplasmic
foci.
action: ACCEPT
reason: IDA annotation from the foundational CAR-1 characterization paper.
This study established CAR-1 as a P-body component.
supported_by:
- reference_id: PMID:16267265
supporting_text: Nov 2. CAR-1, a protein that localizes with the mRNA
decapping component DCAP-1, is required for cytokinesis and ER
organization in Caenorhabditis elegans embryos.
- term:
id: GO:0005737
label: cytoplasm
evidence_type: IDA
original_reference_id: PMID:16221731
review:
summary: CAR-1 localizes to cytoplasmic particles in the gonad and early
embryo.
action: ACCEPT
reason: IDA annotation is well-supported. CAR-1 is primarily a cytoplasmic
protein that localizes to various RNP granules.
supported_by:
- reference_id: PMID:16221731
supporting_text: A conserved RNA-protein complex component involved in
physiological germline apoptosis regulation in C.
- term:
id: GO:0005737
label: cytoplasm
evidence_type: IDA
original_reference_id: PMID:16267265
review:
summary: CAR-1 localizes to cytoplasmic foci and P-granules.
action: ACCEPT
reason: IDA annotation is correct. CAR-1 is a cytoplasmic protein.
supported_by:
- reference_id: PMID:16267265
supporting_text: Nov 2. CAR-1, a protein that localizes with the mRNA
decapping component DCAP-1, is required for cytokinesis and ER
organization in Caenorhabditis elegans embryos.
- term:
id: GO:0043186
label: P granule
evidence_type: IDA
original_reference_id: PMID:16221731
review:
summary: CAR-1 localizes to P granules and associates with CGH-1 in a
conserved germline RNP complex.
action: ACCEPT
reason: IDA annotation is well-supported. P-granule localization is a core
aspect of CAR-1 function in the germline.
supported_by:
- reference_id: PMID:16221731
supporting_text: A conserved RNA-protein complex component involved in
physiological germline apoptosis regulation in C.
- term:
id: GO:0043186
label: P granule
evidence_type: IDA
original_reference_id: PMID:16247027
review:
summary: CAR-1 localizes to P-granules that concentrate in germline
precursors. P-granule localization is confirmed by colocalization with
PGL-1.
action: ACCEPT
reason: IDA annotation is well-supported. CAR-1 localizes to
RNA-containing P-granules that concentrate in the germline precursors
(PMID:16247027).
supported_by:
- reference_id: PMID:16247027
supporting_text: A complex containing the Sm protein CAR-1 and the RNA
helicase CGH-1 is required for embryonic cytokinesis in
Caenorhabditis elegans.
- term:
id: GO:0043186
label: P granule
evidence_type: IDA
original_reference_id: PMID:16267265
review:
summary: Original characterization showing CAR-1 localization to
P-granules.
action: ACCEPT
reason: IDA annotation from foundational CAR-1 paper. P-granule
localization is central to CAR-1 germline function.
supported_by:
- reference_id: PMID:16267265
supporting_text: Nov 2. CAR-1, a protein that localizes with the mRNA
decapping component DCAP-1, is required for cytokinesis and ER
organization in Caenorhabditis elegans embryos.
- term:
id: GO:0000281
label: mitotic cytokinesis
evidence_type: IMP
original_reference_id: PMID:16247027
review:
summary: CAR-1 is essential for embryonic cytokinesis. car-1(RNAi) and
car-1 mutant embryos fail to complete cytokinesis, with cleavage furrows
regressing and spindle midzone failing to form.
action: NEW
reason: This is a core function of CAR-1 not explicitly annotated. CAR-1
was named for Cytokinesis, Apoptosis, RNA-associated reflecting its
essential role in cytokinesis. Multiple studies demonstrate cytokinesis
failure upon CAR-1 depletion.
supported_by:
- reference_id: PMID:16247027
supporting_text: A complex containing the Sm protein CAR-1 and the RNA
helicase CGH-1 is required for embryonic cytokinesis in
Caenorhabditis elegans.
- term:
id: GO:0017148
label: negative regulation of translation
evidence_type: IBA
original_reference_id: GO_REF:0000033
review:
summary: CAR-1 functions in translational repression as part of P-body and
OMA RNP complexes. CAR-1 is part of the IFET-1/CGH-1/CAR-1/PATR-1
repressive complex.
action: NEW
reason: This is a core molecular function of CAR-1 based on phylogenetic
conservation and its role in P-body-mediated mRNA regulation. CAR-1
associates with translational repressors in OMA RNPs (PMID:25261697).
- term:
id: GO:0043066
label: negative regulation of apoptotic process
evidence_type: IMP
original_reference_id: PMID:16221731
review:
summary: CAR-1 regulates physiological germline apoptosis. car-1(RNAi)
leads to increased germline cell death, indicating CAR-1 normally
suppresses apoptosis.
action: NEW
reason: This is a core function of CAR-1 (the A in CAR-1 stands for
Apoptosis). Depletion of CAR-1 increases physiological germline
apoptosis, demonstrating a negative regulatory role.
supported_by:
- reference_id: PMID:16221731
supporting_text: A conserved RNA-protein complex component involved in
physiological germline apoptosis regulation in C.
references:
- id: GO_REF:0000033
title: Annotation inferences using phylogenetic trees
findings:
- statement: CAR-1 is orthologous to LSM14 family proteins across
eukaryotes
- id: GO_REF:0000043
title: Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword
mapping
findings: []
- id: GO_REF:0000044
title: Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular
Location vocabulary mapping
findings: []
- id: GO_REF:0000117
title: Electronic Gene Ontology annotations created by ARBA machine learning
models
findings: []
- id: GO_REF:0000120
title: Combined Automated Annotation using Multiple IEA Methods
findings: []
- id: PMID:16221731
title: A conserved RNA-protein complex component involved in physiological
germline apoptosis regulation in C. elegans.
findings:
- statement: CAR-1 associates with CGH-1 and Y-box proteins in a conserved
germline RNP complex
- statement: The CGH-1/CAR-1 interaction is conserved in Drosophila
oocytes
- statement: car-1(RNAi) increases physiological germline apoptosis
- statement: CAR-1 is critical for oogenesis
- id: PMID:16247027
title: A complex containing the Sm protein CAR-1 and the RNA helicase CGH-1
is required for embryonic cytokinesis in Caenorhabditis elegans.
findings:
- statement: CAR-1 contains an atypical Sm domain and RGG box that bind
RNA
- statement: CAR-1 forms an RNA-dependent complex with CGH-1 and CEY-2
- statement: CAR-1 localizes to P-granules and smaller cytoplasmic
particles
- statement: The Sm domain is essential for CAR-1 function but not
localization
- statement: CAR-1 depletion causes failure of interzonal microtubule
bundle formation
- statement: CAR-1 depletion prevents AIR-2 and ZEN-4 targeting to spindle
midzone
- statement: CGH-1 controls CAR-1 particle localization
- id: PMID:16267265
title: CAR-1, a protein that localizes with the mRNA decapping component
DCAP-1, is required for cytokinesis and ER organization in Caenorhabditis
elegans embryos.
findings:
- statement: CAR-1 colocalizes with DCAP-1 in P-bodies
- statement: CAR-1 localizes to P-granules
- statement: car-1 inhibition causes late cytokinesis failures
- statement: Spindle midzone fails to form in car-1 depleted embryos
- statement: ER organization is disrupted in car-1 depleted embryos
- id: PMID:18430416
title: Involvement of HMG-12 and CAR-1 in the cdc-48.1 expression of
Caenorhabditis elegans.
findings:
- statement: CAR-1 was identified as binding to Element B in cdc-48.1
promoter
- statement: car-1(RNAi) decreases cdc-48.1 and cdc-48.2 expression in
embryos
- id: PMID:18515547
title: C. elegans La-related protein, LARP-1, localizes to germline P bodies
and attenuates Ras-MAPK signaling during oogenesis.
findings:
- statement: LARP-1 colocalizes with P bodies containing CAR-1
- id: PMID:24367695
title: PAB-1, a Caenorhabditis elegans poly(A)-binding protein, regulates
mRNA metabolism in germline by interacting with CGH-1 and CAR-1.
findings:
- statement: PAB-1 colocalizes with CAR-1 in P-granules and P-bodies
- statement: PAB-1, CGH-1, and CAR-1 interact in mRNA metabolism
regulation
- statement: CGH-1 controls CAR-1 localization; CAR-1 does not control
CGH-1 localization
- statement: PAB-1 affects CGH-1 and CAR-1 localization
- id: PMID:25261697
title: Translational control of the oogenic program by components of OMA
ribonucleoprotein particles in Caenorhabditis elegans.
findings:
- statement: CAR-1 is a component of OMA-1 ribonucleoprotein particles
- statement: OMA RNPs contain translational repressors and activators
core_functions:
- description: CAR-1 is an mRNA-binding protein that functions in
post-transcriptional regulation of maternally loaded mRNAs. It directly
binds RNA through its atypical Sm domain and RGG box. CAR-1 forms an
RNA-dependent complex with CGH-1 (DDX6 homolog) and CEY-2, functioning in
P-body and P-granule mediated mRNA regulation. It is essential for
embryonic cytokinesis and regulates physiological germline apoptosis.
molecular_function:
id: GO:0003729
label: mRNA binding
directly_involved_in:
- id: GO:0000281
label: mitotic cytokinesis
- id: GO:0043066
label: negative regulation of apoptotic process
- id: GO:0017148
label: negative regulation of translation
locations:
- id: GO:0043186
label: P granule
- id: GO:0000932
label: P-body
in_complex:
id: GO:1990904
label: ribonucleoprotein complex
proposed_new_terms: []
suggested_questions:
- question: Is CAR-1's role in transcriptional regulation of cdc-48.1
(PMID:18430416) a true transcriptional function or an indirect effect
through mRNA regulation?
- question: What specific mRNAs does CAR-1 regulate to control cytokinesis and
anaphase spindle structure?
- question: Does CAR-1 play a direct role in piRNA silencing pathways as
suggested by some studies of CAR-1/CGH-1 function?
suggested_experiments:
- description: CLIP-seq or RIP-seq to identify direct CAR-1 mRNA targets in
embryos and germline.
- description: Determine whether CAR-1's effect on cdc-48.1 expression is at
the transcriptional or post-transcriptional level.
- description: Characterize the specific mRNAs regulated by CAR-1 that are
required for interzonal microtubule bundle formation.
tags:
- caeel-p-granules