DYNLT2B

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0000922 spindle pole	IDA PMID:25830415 Tctex1d2 associates with short-rib polydactyly syndrome prot...	KEEP AS NON CORE	Summary: Spindle-pole localization was observed during cell division; this is a secondary localization alongside the core ciliary dynein-2 role. Reason: Spindle-pole localization was observed during cell division; this is a secondary localization alongside the core ciliary dynein-2 role. Supporting Evidence: PMID:25830415 Tctex1d2 associates with Wdr34, Wdr60, and other subunits of Dync1 and Dync2 and colocalizes with Wdr60 to microtubule organizing centers during interphase, the mitotic spindle poles during cell division, and the base of the cilium in ciliated cells.
GO:0001673 male germ cell nucleus	NAS PMID:36973253 Distinct dynein complexes defined by DYNLRB1 and DYNLRB2 reg...	MARK AS OVER ANNOTATED	Summary: Complex-level NAS from ComplexPortal; the cited paper does not examine DYNLT2B, and no study places this dynein-2 light chain in the male germ cell nucleus. Reason: The cached full text of PMID:36973253 analyses DYNLRB1- and DYNLRB2-defined dynein complexes in mitotic and male meiotic spindles and does not mention DYNLT2B/TCTEX1D2. The annotation is a statement inferred from a complex description, not an observation on this protein, and nuclear residence is not consistent with what is known of dynein-2 (ciliary base, MTOC, axoneme). Mouse testis data place TCTEX1D2 in the sperm flagellar axoneme, not the nucleus. The term overstates the evidence for this gene product. Supporting Evidence: PMID:39827215 TCTEX1D2 is an axoneme component and interacts with subunits of inner dynein arm
GO:0005515 protein binding	IPI PMID:20195357 A comprehensive resource of interacting protein regions for ...	REMOVE	Summary: Bare protein binding to GTF2F2 from a high-throughput binary interaction screen; uninformative. Reason: Generic protein binding carries no functional information. The GTF2F2 interaction comes from a proteome-scale screen, has no follow-up linking it to dynein-2 or ciliary function, and does not support a more informative molecular function term. Removal does not assert that the reported interaction is false.
GO:0005515 protein binding	IPI PMID:25910212 Widespread macromolecular interaction perturbations in human...	REMOVE	Summary: Bare protein binding to ACTN2 from a high-throughput binary interaction screen; uninformative. Reason: Generic protein binding carries no functional information. The ACTN2 interaction comes from a proteome-scale screen, has no follow-up linking it to dynein-2 or ciliary function, and does not support a more informative molecular function term. Removal does not assert that the reported interaction is false.
GO:0005515 protein binding	IPI PMID:26044572 TCTEX1D2 mutations underlie Jeune asphyxiating thoracic dyst...	MODIFY	Summary: The partner is the dynein-2 intermediate chain WDR60 (DYNC2I1); the informative term is dynein intermediate chain binding. Reason: Affinity purification of tagged TCTEX1D2 recovered the IFT-dynein intermediate chains WDR34 and WDR60, and follow-up work mapped the TCTEX1D2-DYNLT1/DYNLT3 dimer onto WDR60. Replace bare protein binding with dynein intermediate chain binding, which the gene already carries by IPI and IBA. Proposed replacements: dynein intermediate chain binding Supporting Evidence: PMID:26044572 We were able to identify interactions of TCTEX1D2 with IFT dynein intermediate chains WDR34 and WDR60, and light chains DYNLT1, DYNLT3 and DYNLRB1 (Supplementary Table 7). PMID:29742051 We established cell lines lacking WDR60 or TCTEX1D2, both of which are dynein-2-specific subunits encoded by ciliopathy-causing genes, and found that both WDR60-knockout (KO) and TCTEX1D2-KO cells show defects in retrograde ciliary protein trafficking, with WDR60-KO cells demonstrating more severe defects probably due to failed assembly of the dynein-2 complex.
GO:0005515 protein binding	IPI PMID:27173435 An organelle-specific protein landscape identifies novel dis...	MODIFY	Summary: The DYNLT1 partner is itself a Tctex-type dynein light chain; the specific activity is dynein light chain binding (heterodimerization with DYNLT1). Reason: DYNLT2B forms an obligate 1:1 heterodimer with the Tctex light chain DYNLT1 within the dynein-2 tail, shown by affinity proteomics, binary interaction screens and an X-ray structure of the DYNLT1-DYNLT2B heterodimer. Bare protein binding should be replaced by dynein light chain binding. Proposed replacements: dynein light chain binding Supporting Evidence: PMID:38454149 X-ray crystallography structure of DYNLT1-DYNLT2B heterodimer. PMID:26044572 We were able to identify interactions of TCTEX1D2 with IFT dynein intermediate chains WDR34 and WDR60, and light chains DYNLT1, DYNLT3 and DYNLRB1 (Supplementary Table 7).
GO:0005515 protein binding	IPI PMID:32296183 A reference map of the human binary protein interactome.	REMOVE	Summary: Bare protein binding to CDKN2D from a high-throughput binary interaction screen; uninformative. Reason: Generic protein binding carries no functional information. The CDKN2D interaction comes from a proteome-scale screen, has no follow-up linking it to dynein-2 or ciliary function, and does not support a more informative molecular function term. Removal does not assert that the reported interaction is false.
GO:0005515 protein binding	IPI PMID:32296183 A reference map of the human binary protein interactome.	MODIFY	Summary: The DYNLT1 partner is itself a Tctex-type dynein light chain; the specific activity is dynein light chain binding (heterodimerization with DYNLT1). Reason: DYNLT2B forms an obligate 1:1 heterodimer with the Tctex light chain DYNLT1 within the dynein-2 tail, shown by affinity proteomics, binary interaction screens and an X-ray structure of the DYNLT1-DYNLT2B heterodimer. Bare protein binding should be replaced by dynein light chain binding. Proposed replacements: dynein light chain binding Supporting Evidence: PMID:38454149 X-ray crystallography structure of DYNLT1-DYNLT2B heterodimer. PMID:26044572 We were able to identify interactions of TCTEX1D2 with IFT dynein intermediate chains WDR34 and WDR60, and light chains DYNLT1, DYNLT3 and DYNLRB1 (Supplementary Table 7).
GO:0005515 protein binding	IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling...	MODIFY	Summary: The DYNLT1 partner is itself a Tctex-type dynein light chain; the specific activity is dynein light chain binding (heterodimerization with DYNLT1). Reason: DYNLT2B forms an obligate 1:1 heterodimer with the Tctex light chain DYNLT1 within the dynein-2 tail, shown by affinity proteomics, binary interaction screens and an X-ray structure of the DYNLT1-DYNLT2B heterodimer. Bare protein binding should be replaced by dynein light chain binding. Proposed replacements: dynein light chain binding Supporting Evidence: PMID:38454149 X-ray crystallography structure of DYNLT1-DYNLT2B heterodimer. PMID:26044572 We were able to identify interactions of TCTEX1D2 with IFT dynein intermediate chains WDR34 and WDR60, and light chains DYNLT1, DYNLT3 and DYNLRB1 (Supplementary Table 7).
GO:0005737 cytoplasm	IBA GO_REF:0000033	KEEP AS NON CORE	Summary: Family-level IBA for cytoplasmic localization; correct, and DYNLT2B is observed at several cytoplasmic microtubule structures, but the functionally defining location is the ciliary base and cilium. Reason: The PAINT node PTN000478852 spans the Tctex light-chain family (DYNLT1, DYNLT3, fly and yeast Tctex members), so cytoplasm is the level at which the family-wide claim was placed. Human TCTEX1D2 is seen at interphase MTOCs, spindle poles and the ciliary base, all cytoplasmic microtubule structures, so the claim holds; the location defining its core role (ciliary base/cilium) is captured by separate rows. Supporting Evidence: PMID:25830415 Tctex1d2 associates with Wdr34, Wdr60, and other subunits of Dync1 and Dync2 and colocalizes with Wdr60 to microtubule organizing centers during interphase, the mitotic spindle poles during cell division, and the base of the cilium in ciliated cells.
GO:0005813 centrosome	IDA PMID:25830415 Tctex1d2 associates with short-rib polydactyly syndrome prot...	KEEP AS NON CORE	Summary: Endogenous TCTEX1D2 colocalizes with WDR60 at centrosomal MTOCs; real but secondary to the ciliary-base/dynein-2 role. Reason: Immunofluorescence in human cells shows the protein at MTOCs/centrosomes during interphase, depending on WDR60 and microtubules. This is consistent with recruitment of dynein-2 to the basal body region but is not itself the core functional location. Supporting Evidence: PMID:25830415 Tctex1d2 associates with Wdr34, Wdr60, and other subunits of Dync1 and Dync2 and colocalizes with Wdr60 to microtubule organizing centers during interphase, the mitotic spindle poles during cell division, and the base of the cilium in ciliated cells.
GO:0005868 cytoplasmic dynein complex	IBA GO_REF:0000033	ACCEPT	Summary: Biochemical isolation and interaction mapping place TCTEX1D2 in cytoplasmic dynein-2; this is complex membership rather than intrinsic ATPase activity. Reason: Biochemical isolation and interaction mapping place TCTEX1D2 in cytoplasmic dynein-2; this is complex membership rather than intrinsic ATPase activity. Supporting Evidence: PMID:25205765 Here, we now also identify the TCTEX1D2 light chain (Tctex-2) as a light chain for dynein-2, not present in dynein-1.
GO:0005868 cytoplasmic dynein complex	IDA PMID:25205765 Subunit composition of the human cytoplasmic dynein-2 comple...	ACCEPT	Summary: Biochemical isolation and interaction mapping place TCTEX1D2 in cytoplasmic dynein-2; this is complex membership rather than intrinsic ATPase activity. Reason: Biochemical isolation and interaction mapping place TCTEX1D2 in cytoplasmic dynein-2; this is complex membership rather than intrinsic ATPase activity. Supporting Evidence: PMID:25205765 Here, we now also identify the TCTEX1D2 light chain (Tctex-2) as a light chain for dynein-2, not present in dynein-1.
GO:0005868 cytoplasmic dynein complex	IDA PMID:25830415 Tctex1d2 associates with short-rib polydactyly syndrome prot...	ACCEPT	Summary: Biochemical isolation and interaction mapping place TCTEX1D2 in cytoplasmic dynein-2; this is complex membership rather than intrinsic ATPase activity. Reason: Biochemical isolation and interaction mapping place TCTEX1D2 in cytoplasmic dynein-2; this is complex membership rather than intrinsic ATPase activity. Supporting Evidence: PMID:25205765 Here, we now also identify the TCTEX1D2 light chain (Tctex-2) as a light chain for dynein-2, not present in dynein-1.
GO:0005929 cilium	NAS PMID:30065109 Emerging mechanisms of dynein transport in the cytoplasm ver...	ACCEPT	Summary: Dynein-2, including DYNLT2B, enters cilia on IFT trains and returns cargo from the tip; cilium is the appropriate location for the complex. Reason: ComplexPortal NAS based on dynein-2 reviews. Independent primary evidence: TCTEX1D2 is an integral IFT-dynein subunit and its loss impairs retrograde IFT; endogenous protein is detected at the ciliary base and tagged protein in the axoneme. Supporting Evidence: PMID:26044572 Affinity proteomics indicates that TCTEX1D2/Tctex2b is an integral component of IFT dynein. We demonstrate a retrograde IFT defect in TCTEX1D2-deficient human fibroblasts and Tctex2b-deficient Chlamydomonas cells, and find that IFT dynein is partially destabilized by loss of Tctex2b in Chlamydomonas.
GO:0005929 cilium	NAS PMID:32229580 Cytoplasmic dynein-2 at a glance.	ACCEPT	Summary: Dynein-2, including DYNLT2B, enters cilia on IFT trains and returns cargo from the tip; cilium is the appropriate location for the complex. Reason: ComplexPortal NAS based on dynein-2 reviews. Independent primary evidence: TCTEX1D2 is an integral IFT-dynein subunit and its loss impairs retrograde IFT; endogenous protein is detected at the ciliary base and tagged protein in the axoneme. Supporting Evidence: PMID:26044572 Affinity proteomics indicates that TCTEX1D2/Tctex2b is an integral component of IFT dynein. We demonstrate a retrograde IFT defect in TCTEX1D2-deficient human fibroblasts and Tctex2b-deficient Chlamydomonas cells, and find that IFT dynein is partially destabilized by loss of Tctex2b in Chlamydomonas.
GO:0005930 axoneme	IDA PMID:25830415 Tctex1d2 associates with short-rib polydactyly syndrome prot...	KEEP AS NON CORE	Summary: Axonemal signal was observed for overexpressed tagged TCTEX1D2; the same study did not detect a clear endogenous axonemal signal. Retain the experimental localization with this limitation. Reason: Axonemal signal was observed for overexpressed tagged TCTEX1D2; the same study did not detect a clear endogenous axonemal signal. Retain the experimental localization with this limitation. Supporting Evidence: PMID:25830415 overexpression of LAP(EGFP-TEV-S-Peptide)-Tctex1d2 led to the localization of LAP-Tctex1d2 to the ciliary axoneme (Fig. 3I), similar to what had been observed with Wdr60 overexpression.4
GO:0007018 microtubule-based movement	IBA GO_REF:0000033	MODIFY	Summary: Correct family-level IBA, but for DYNLT2B the supported specific process is intraciliary retrograde transport, a descendant of microtubule-based movement that the gene already carries by IMP. Reason: The PAINT node covers Tctex light chains of both dynein-1 and dynein-2, so microtubule-based movement is the right generality for the node. For this dynein-2-specific subunit the experimentally supported process is retrograde IFT (human KO fibroblasts and Chlamydomonas Tctex2b mutants), and GO:0035721 is_a descendant of microtubule-based movement. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: PANTHER:PTN000478852 SUPPORTS TRANSFER Tctex light-chain family node spanning dynein-1 (DYNLT1/DYNLT3, fly Tctex-1, fission yeast) and dynein-2 (DYNLT2B) members; microtubule-based movement is the right generality for the node, and the target is inside the clade. The term is correct for DYNLT2B but the specific process it contributes to is intraciliary retrograde transport. UniProtKB:Q8WW35 SUPPORTS TRANSFER Target's own retrograde-IFT loss-of-function evidence is among the descendant evidences; not circular. Proposed replacements: intraciliary retrograde transport Supporting Evidence: PMID:26044572 Affinity proteomics indicates that TCTEX1D2/Tctex2b is an integral component of IFT dynein. We demonstrate a retrograde IFT defect in TCTEX1D2-deficient human fibroblasts and Tctex2b-deficient Chlamydomonas cells, and find that IFT dynein is partially destabilized by loss of Tctex2b in Chlamydomonas.
GO:0030286 dynein complex	NAS PMID:30065109 Emerging mechanisms of dynein transport in the cytoplasm ver...	MODIFY	Summary: Correct but general; DYNLT2B belongs to cytoplasmic dynein-2, captured by the more specific cytoplasmic dynein complex term the gene already carries by IDA. Reason: The established complex is cytoplasmic dynein-2 (IFT dynein). GO:0005868 cytoplasmic dynein complex is the specific descendant supported by affinity proteomics and is already annotated to the gene. Proposed replacements: cytoplasmic dynein complex Supporting Evidence: PMID:25205765 Here, we now also identify the TCTEX1D2 light chain (Tctex-2) as a light chain for dynein-2, not present in dynein-1.
GO:0030286 dynein complex	NAS PMID:32229580 Cytoplasmic dynein-2 at a glance.	MODIFY	Summary: Correct but general; DYNLT2B belongs to cytoplasmic dynein-2, captured by the more specific cytoplasmic dynein complex term the gene already carries by IDA. Reason: The established complex is cytoplasmic dynein-2 (IFT dynein). GO:0005868 cytoplasmic dynein complex is the specific descendant supported by affinity proteomics and is already annotated to the gene. Proposed replacements: cytoplasmic dynein complex Supporting Evidence: PMID:25205765 Here, we now also identify the TCTEX1D2 light chain (Tctex-2) as a light chain for dynein-2, not present in dynein-1.
GO:0031021 interphase microtubule organizing center	IDA PMID:25830415 Tctex1d2 associates with short-rib polydactyly syndrome prot...	KEEP AS NON CORE	Summary: The interphase microtubule-organizing-center localization is directly observed, but its role is less specific than ciliary-base recruitment. Reason: The interphase microtubule-organizing-center localization is directly observed, but its role is less specific than ciliary-base recruitment. Supporting Evidence: PMID:25830415 Tctex1d2 associates with Wdr34, Wdr60, and other subunits of Dync1 and Dync2 and colocalizes with Wdr60 to microtubule organizing centers during interphase, the mitotic spindle poles during cell division, and the base of the cilium in ciliated cells.
GO:0035721 intraciliary retrograde transport	IMP PMID:29742051 Interaction of WDR60 intermediate chain with TCTEX1D2 light ...	ACCEPT	Summary: TCTEX1D2-KO human cells show defects in retrograde ciliary protein trafficking; DYNLT2B is a structural subunit of the motor that executes this process. Reason: Direct loss-of-function evidence in human cells, corroborated by patient fibroblasts and the Chlamydomonas ortholog. DYNLT2B contributes structure to the dynein-2 tail (WDR60 arm) rather than ATPase activity, which qualifies as participation in the process. Supporting Evidence: PMID:29742051 We established cell lines lacking WDR60 or TCTEX1D2, both of which are dynein-2-specific subunits encoded by ciliopathy-causing genes, and found that both WDR60-knockout (KO) and TCTEX1D2-KO cells show defects in retrograde ciliary protein trafficking, with WDR60-KO cells demonstrating more severe defects probably due to failed assembly of the dynein-2 complex. PMID:26044572 Affinity proteomics indicates that TCTEX1D2/Tctex2b is an integral component of IFT dynein. We demonstrate a retrograde IFT defect in TCTEX1D2-deficient human fibroblasts and Tctex2b-deficient Chlamydomonas cells, and find that IFT dynein is partially destabilized by loss of Tctex2b in Chlamydomonas.
GO:0035721 intraciliary retrograde transport	NAS PMID:31451806 Structure of the dynein-2 complex and its assembly with intr...	ACCEPT	Summary: DYNLT2B is an integral subunit of the retrograde IFT dynein; consistent with direct loss-of-function evidence. Reason: ComplexPortal NAS for the dynein-2 complex. Supported independently by human TCTEX1D2-deficient fibroblasts and KO cells showing retrograde IFT defects and by Chlamydomonas Tctex2b mutants showing destabilized IFT dynein. Supporting Evidence: PMID:26044572 Affinity proteomics indicates that TCTEX1D2/Tctex2b is an integral component of IFT dynein. We demonstrate a retrograde IFT defect in TCTEX1D2-deficient human fibroblasts and Tctex2b-deficient Chlamydomonas cells, and find that IFT dynein is partially destabilized by loss of Tctex2b in Chlamydomonas. PMID:29742051 We established cell lines lacking WDR60 or TCTEX1D2, both of which are dynein-2-specific subunits encoded by ciliopathy-causing genes, and found that both WDR60-knockout (KO) and TCTEX1D2-KO cells show defects in retrograde ciliary protein trafficking, with WDR60-KO cells demonstrating more severe defects probably due to failed assembly of the dynein-2 complex.
GO:0035721 intraciliary retrograde transport	NAS PMID:32229580 Cytoplasmic dynein-2 at a glance.	ACCEPT	Summary: DYNLT2B is an integral subunit of the retrograde IFT dynein; consistent with direct loss-of-function evidence. Reason: ComplexPortal NAS for the dynein-2 complex. Supported independently by human TCTEX1D2-deficient fibroblasts and KO cells showing retrograde IFT defects and by Chlamydomonas Tctex2b mutants showing destabilized IFT dynein. Supporting Evidence: PMID:26044572 Affinity proteomics indicates that TCTEX1D2/Tctex2b is an integral component of IFT dynein. We demonstrate a retrograde IFT defect in TCTEX1D2-deficient human fibroblasts and Tctex2b-deficient Chlamydomonas cells, and find that IFT dynein is partially destabilized by loss of Tctex2b in Chlamydomonas. PMID:29742051 We established cell lines lacking WDR60 or TCTEX1D2, both of which are dynein-2-specific subunits encoded by ciliopathy-causing genes, and found that both WDR60-knockout (KO) and TCTEX1D2-KO cells show defects in retrograde ciliary protein trafficking, with WDR60-KO cells demonstrating more severe defects probably due to failed assembly of the dynein-2 complex.
GO:0045505 dynein intermediate chain binding	IBA GO_REF:0000033	ACCEPT	Summary: The TCTEX1D2–DYNLT1/DYNLT3 dimer interacts with the dynein-2 intermediate chain WDR60. This is a specific functional interaction. Reason: The TCTEX1D2–DYNLT1/DYNLT3 dimer interacts with the dynein-2 intermediate chain WDR60. This is a specific functional interaction. Supporting Evidence: PMID:29742051 Utilizing the visible immunoprecipitation assay, we demonstrated the interaction modes among the dynein-2 subunits, including previously undefined interactions, such as that between WDR60 and the TCTEX1D2-DYNLT1/DYNLT3 dimer. The dynein-2 complex can be divided into three subcomplexes, namely DYNC2H1-DYNC2LI1, WDR34-DYNLL1/DYNLL2-DYNLRB1/DYNLRB2, and WDR60-TCTEX1D2-DYNLT1/DYNLT3.
GO:0045505 dynein intermediate chain binding	IPI PMID:25830415 Tctex1d2 associates with short-rib polydactyly syndrome prot...	ACCEPT	Summary: The TCTEX1D2–DYNLT1/DYNLT3 dimer interacts with the dynein-2 intermediate chain WDR60. This is a specific functional interaction. Reason: The TCTEX1D2–DYNLT1/DYNLT3 dimer interacts with the dynein-2 intermediate chain WDR60. This is a specific functional interaction. Supporting Evidence: PMID:29742051 Utilizing the visible immunoprecipitation assay, we demonstrated the interaction modes among the dynein-2 subunits, including previously undefined interactions, such as that between WDR60 and the TCTEX1D2-DYNLT1/DYNLT3 dimer. The dynein-2 complex can be divided into three subcomplexes, namely DYNC2H1-DYNC2LI1, WDR34-DYNLL1/DYNLL2-DYNLRB1/DYNLRB2, and WDR60-TCTEX1D2-DYNLT1/DYNLT3.
GO:0045505 dynein intermediate chain binding	IPI PMID:25830415 Tctex1d2 associates with short-rib polydactyly syndrome prot...	ACCEPT	Summary: The TCTEX1D2–DYNLT1/DYNLT3 dimer interacts with the dynein-2 intermediate chain WDR60. This is a specific functional interaction. Reason: The TCTEX1D2–DYNLT1/DYNLT3 dimer interacts with the dynein-2 intermediate chain WDR60. This is a specific functional interaction. Supporting Evidence: PMID:29742051 Utilizing the visible immunoprecipitation assay, we demonstrated the interaction modes among the dynein-2 subunits, including previously undefined interactions, such as that between WDR60 and the TCTEX1D2-DYNLT1/DYNLT3 dimer. The dynein-2 complex can be divided into three subcomplexes, namely DYNC2H1-DYNC2LI1, WDR34-DYNLL1/DYNLL2-DYNLRB1/DYNLRB2, and WDR60-TCTEX1D2-DYNLT1/DYNLT3.
GO:0060271 cilium assembly	IMP PMID:25830415 Tctex1d2 associates with short-rib polydactyly syndrome prot...	KEEP AS NON CORE	Summary: Depletion impairs ciliogenesis in human cells; consistent with dynein-2/IFT being required for cilium assembly, but this is a downstream consequence of the core retrograde-IFT role. Reason: Intraciliary transport is part of cilium assembly in GO and the IMP is curator-made from full text (siRNA depletion reduced ciliogenesis in that study). Other studies found milder effects (TCTEX1D2-depleted cells still form cilia but they are longer, PMID:25205765; mild trafficking defects in KO cells, PMID:29742051), so this is a context-dependent downstream outcome of the core retrograde-IFT role and is kept as non-core. Supporting Evidence: PMID:25830415 Tctex1d2 and Wdr60 localize to the base of the cilium and their depletion causes defects in ciliogenesis.
GO:0097546 ciliary base	IDA PMID:25830415 Tctex1d2 associates with short-rib polydactyly syndrome prot...	ACCEPT	Summary: Human microscopy places endogenous TCTEX1D2 at the ciliary base, consistent with dynein-2 recruitment. Reason: Human microscopy places endogenous TCTEX1D2 at the ciliary base, consistent with dynein-2 recruitment. Supporting Evidence: PMID:25830415 Tctex1d2 associates with Wdr34, Wdr60, and other subunits of Dync1 and Dync2 and colocalizes with Wdr60 to microtubule organizing centers during interphase, the mitotic spindle poles during cell division, and the base of the cilium in ciliated cells.
GO:0120293 dynein axonemal particle	IEA GO_REF:0000044	UNDECIDED	Summary: SubCell mapping from a curator-inferred UniProt location (ECO:0000305). No study tested DYNLT2B residence in dynein axonemal particles; mouse and Chlamydomonas data suggest an inner-arm axonemal role that makes it plausible but unshown. Reason: Dynein axonemal particles are cytoplasmic preassembly foci for axonemal dyneins. The mouse study reports TCTEX1D2 as a sperm axoneme component interacting with inner-dynein-arm intermediate chains WDR63 and WDR78, and Chlamydomonas Tctex2b is an inner-arm light chain, so passage through DAPs is plausible for this axonemal pool. No experiment localizes the protein to DAPs, so the call is left open. Supporting Evidence: PMID:39827215 TCTEX1D2 is an axoneme component and interacts with subunits of inner dynein arm
GO:1902017 regulation of cilium assembly	IMP PMID:25205765 Subunit composition of the human cytoplasmic dynein-2 comple...	KEEP AS NON CORE	Summary: TCTEX1D2 depletion lengthens cilia without blocking their formation; a downstream consequence of impaired retrograde IFT, retained as non-core. Reason: In the cited study TCTEX1D2 depletion did not prevent ciliogenesis but significantly increased cilia length, a phenotype typical of impaired retrograde IFT. The curator-made IMP is not contradicted and fits a ciliary-length (assembly control) effect, but it is a downstream consequence of the gene's role as a dynein-2 subunit rather than a dedicated regulatory activity, so it is non-core. Supporting Evidence: PMID:25205765 In all cases, we can detect a statistically significant increase in cilia length following TCTEX1D2 depletion. PMID:25205765 Of note, TCTEX1D2-depleted cells still form cilia.
GO:1905799 regulation of intraciliary retrograde transport	IMP PMID:26044572 TCTEX1D2 mutations underlie Jeune asphyxiating thoracic dyst...	MODIFY	Summary: DYNLT2B is a subunit of the IFT dynein that performs retrograde IFT; its loss impairs the process itself, so participation (intraciliary retrograde transport) is the appropriate term rather than regulation. Reason: Loss of TCTEX1D2/Tctex2b impairs retrograde IFT and partially destabilizes the IFT dynein motor. That is evidence that the protein is part of the machinery executing the process, not that it modulates the rate of a process carried out by others. Lateral correction to GO:0035721, which the gene already carries by IMP. Proposed replacements: intraciliary retrograde transport Supporting Evidence: PMID:26044572 Affinity proteomics indicates that TCTEX1D2/Tctex2b is an integral component of IFT dynein. We demonstrate a retrograde IFT defect in TCTEX1D2-deficient human fibroblasts and Tctex2b-deficient Chlamydomonas cells, and find that IFT dynein is partially destabilized by loss of Tctex2b in Chlamydomonas.

Gene Description

Existing Annotations Review

Core Functions

Structural light-chain subunit of cytoplasmic dynein-2: as a heterodimer with DYNLT1/DYNLT3 it binds the WDR60 intermediate chain in the dynein-2 tail and is required for stable motor function in retrograde intraflagellar transport.

Heterodimerization with the Tctex light chain DYNLT1 (dynein light chain binding), forming the light-chain pair that docks onto the dynein-2 intermediate chains.

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