COPS8 (CSN8) encodes the eighth subunit of the COP9 signalosome (CSN), an evolutionarily conserved eight-subunit protein complex. COPS8 is a PCI-domain scaffold subunit essential for CSN holocomplex integrity and stability. The CSN complex functions as a master regulator of cullin-RING E3 ligases (CRLs) through its deneddylation activity, removing the ubiquitin-like modifier NEDD8 from cullin scaffolds. While COPS8 itself does not possess catalytic activity (the deneddylase activity resides in CSN5/JAB1), it is required for proper complex assembly and function. CSN8 hypomorphism destabilizes the CSN holocomplex and leads to formation of cytoplasmic CSN5 mini-complexes. The protein localizes to both cytoplasm and nucleus where the CSN complex regulates CRL-dependent protein turnover affecting signaling pathways including p53, c-Jun/AP-1, and NF-kappaB/IkappaBalpha.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0008180 COP9 signalosome | IBA GO_REF:0000033 | ACCEPT | Summary: COPS8 is an integral subunit of the COP9 signalosome complex. This is well-established from multiple studies including the original characterization (PMID:9535219) and structural studies (PMID:18850735, PMID:25043011). The IBA annotation is consistent with phylogenetic conservation of CSN8 as a core CSN component. Reason: Core function. COPS8 is definitionally a subunit of the COP9 signalosome. The complex consists of eight subunits (GPS1/COPS1, COPS2-8, and COPS9) and COPS8 is essential for holocomplex integrity. This is supported by multiple experimental studies. Supporting Evidence: PMID:9535219 A novel protein complex has been identified in human cells that has a molecular mass of approximately 450 kDa. It consists of at least eight different subunits including JAB1, the Jun activation-domain binding protein 1, and Trip15 PMID:18850735 Purification of the human CSN complex from a stable 293 cell line expressing N-terminal HBTH-tagged CSN5 subunit was achieved by high-affinity streptavidin binding with TEV cleavage elution. |
| GO:0000338 protein deneddylation | IEA GO_REF:0000002 | ACCEPT | Summary: The CSN complex mediates protein deneddylation, removing NEDD8 from cullin substrates. While COPS8 itself lacks deneddylase catalytic activity (which resides in CSN5), it is required for CSN holocomplex integrity and thus for deneddylation function. The IEA annotation from InterPro is appropriate as a broader functional annotation. Reason: The CSN complex functions as the major deneddylase in cells. COPS8 is required for proper CSN complex assembly and therefore contributes to the deneddylation process, even though it does not contain the catalytic metalloprotease domain (found in CSN5). Supporting Evidence: PMID:19141280 The COP9 signalosome (CSN) is an eight-subunit protein complex that is found in all eukaryotes. Accumulating evidence indicates its diverse biological functions that are often linked to ubiquitin-mediated proteolysis... the catalytically active human complex, reconstituted in vitro, is composed of a single copy of each of the eight subunits. |
| GO:0005634 nucleus | IEA GO_REF:0000120 | ACCEPT | Summary: COPS8 and the CSN complex localize to both nucleus and cytoplasm. This IEA annotation is consistent with experimental evidence showing nuclear localization of the CSN. Reason: Correct localization. Multiple experimental studies confirm nuclear localization of the CSN complex and COPS8 (PMID:9535219, PMID:24421388). Supporting Evidence: PMID:24421388 the complex is localized in the cytoplasm, nucleoplasm, and chromatin-bound fractions, each differing in the composition of posttranslationally modified subunits, depending on its location within the cell. |
| GO:0005737 cytoplasm | IEA GO_REF:0000044 | ACCEPT | Summary: COPS8 and the CSN complex localize to both nucleus and cytoplasm. This IEA annotation is consistent with experimental evidence from UniProt subcellular location mapping. Reason: Correct localization. Cytoplasmic localization is well-documented for CSN complex (PMID:9535219, PMID:24421388). Supporting Evidence: PMID:9535219 Immunofluorescence staining reveals that the new complex shows a subcellular distribution similar to that of the 26S proteasome. |
| GO:0008180 COP9 signalosome | IEA GO_REF:0000120 | ACCEPT | Summary: Duplicate annotation of COP9 signalosome membership via automated pipeline. This is correct but redundant with the IBA annotation. Reason: Core function. Duplicate annotations with different evidence codes are acceptable. This IEA annotation correctly identifies COPS8 as a CSN subunit. Supporting Evidence: PMID:18850735 Mass spectrometric analysis of the purified CSN complex has revealed the identity of its composition as well as N-terminal modification and phosphorylation of the CSN subunits. |
| GO:0010387 COP9 signalosome assembly | IEA GO_REF:0000002 | ACCEPT | Summary: COPS8 is required for CSN holocomplex assembly and stability. CSN8 hypomorphism leads to destabilization of the CSN complex with formation of CSN5-containing mini-complexes. Reason: CSN8 is essential for proper CSN complex assembly. Studies show that reduced CSN8 levels lead to holocomplex destabilization and formation of aberrant subcomplexes. Supporting Evidence: PMID:23689509 By characterizing the mouse embryonic fibroblasts (MEFs) that express Csn8 at a low level, we found that Csn8 plays an important role in maintaining the proper duration of the G1 phase of the cell cycle. |
| GO:0005515 protein binding | IPI PMID:15304329 Hepatopoietin interacts directly with COP9 signalosome and r... | MODIFY | Summary: This protein binding annotation is too vague. The cited paper shows hepatopoietin interacts with COP9 signalosome components. While the physical interaction may be valid, 'protein binding' does not convey useful functional information about COPS8's role as a structural scaffold subunit. Reason: 'Protein binding' is uninformative. COPS8 functions as a structural scaffold within the CSN complex. A more informative term would describe its role in the complex. Proposed replacements: molecular adaptor activity Supporting Evidence: PMID:15304329 Hepatopoietin interacts directly with COP9 signalosome and regulates AP-1 activity. |
| GO:0005515 protein binding | IPI PMID:18850735 Characterization of the human COP9 signalosome complex using... | MODIFY | Summary: This paper characterizes CSN complex composition and subunit interactions. The protein binding annotation is too vague - COPS8 specifically interacts with other CSN subunits (particularly COPS3, COPS4, COPS7) as part of the complex architecture. Reason: 'Protein binding' is uninformative. The interaction is part of CSN complex formation. Proposed replacements: molecular adaptor activity Supporting Evidence: PMID:18850735 Purification of the human CSN complex from a stable 293 cell line expressing N-terminal HBTH-tagged CSN5 subunit was achieved by high-affinity streptavidin binding with TEV cleavage elution. |
| GO:0005515 protein binding | IPI PMID:19615732 Defining the human deubiquitinating enzyme interaction lands... | MARK AS OVER ANNOTATED | Summary: High-throughput interactome study identifying deubiquitinating enzyme interactions. 'Protein binding' is too vague to be informative. Reason: High-throughput study with generic 'protein binding' term that does not convey specific functional information about COPS8. Supporting Evidence: PMID:19615732 Defining the human deubiquitinating enzyme interaction landscape. |
| GO:0005515 protein binding | IPI PMID:20399188 Structural insights into the COP9 signalosome and its common... | MODIFY | Summary: Structural study of CSN complex. The protein binding annotation reflects structural interactions within the CSN complex but is too vague. Reason: 'Protein binding' is uninformative. The structural analysis shows COPS8 interacts with other CSN subunits as part of the complex architecture. Proposed replacements: molecular adaptor activity Supporting Evidence: PMID:20399188 Structural insights into the COP9 signalosome and its common architecture with the 26S proteasome lid and eIF3. |
| GO:0005515 protein binding | IPI PMID:21145461 Dynamics of cullin-RING ubiquitin ligase network revealed by... | ACCEPT | Summary: Quantitative proteomics study of cullin-RING ligase network dynamics. The interactions detected are relevant to CSN function in regulating CRLs but 'protein binding' is too vague. Reason: The study provides evidence for CSN complex interactions with cullins, which is relevant to its core function. While 'protein binding' is vague, it captures the physical interaction aspect of CSN-CRL regulation. Supporting Evidence: PMID:21145461 Dynamics of cullin-RING ubiquitin ligase network revealed by systematic quantitative proteomics. |
| GO:0005515 protein binding | IPI PMID:24421388 Dynamic regulation of the COP9 signalosome in response to DN... | ACCEPT | Summary: This study examined CSN dynamics in response to DNA damage. The protein binding annotation captures interactions within the complex. Reason: This annotation reflects CSN subunit interactions which are functionally relevant for the complex's role in DNA damage response. Supporting Evidence: PMID:24421388 The COP9 signalosome (CSN) is an evolutionarily conserved protein complex that participates in the regulation of the ubiquitin/26S proteasome pathway |
| GO:0005515 protein binding | IPI PMID:24981860 Human-chromatin-related protein interactions identify a deme... | MARK AS OVER ANNOTATED | Summary: Chromatin-related protein interaction study. 'Protein binding' is too generic. Reason: High-throughput study with generic annotation that does not provide specific functional insight into COPS8. Supporting Evidence: PMID:24981860 Human-chromatin-related protein interactions identify a demethylase complex required for chromosome segregation. |
| GO:0005515 protein binding | IPI PMID:25043011 Crystal structure of the human COP9 signalosome. | MODIFY | Summary: Crystal structure of human COP9 signalosome. The structural analysis reveals COPS8 interactions with other CSN subunits. 'Protein binding' is too vague. Reason: The crystal structure shows COPS8 structural interactions but 'protein binding' is uninformative. The molecular adaptor activity term better captures COPS8's role. Proposed replacements: molecular adaptor activity Supporting Evidence: PMID:25043011 Crystal structure of the human COP9 signalosome. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | MARK AS OVER ANNOTATED | Summary: Large-scale proteome interactome map. Generic 'protein binding' annotation. Reason: High-throughput interactome study. The generic term does not convey functional information specific to COPS8. Supporting Evidence: PMID:25416956 A proteome-scale map of the human interactome network. |
| GO:0005515 protein binding | IPI PMID:26496610 A human interactome in three quantitative dimensions organiz... | MARK AS OVER ANNOTATED | Summary: Quantitative human interactome study. Generic annotation from high-throughput data. Reason: High-throughput study with generic annotation. Supporting Evidence: PMID:26496610 A human interactome in three quantitative dimensions organized by stoichiometries and abundances. |
| GO:0005515 protein binding | IPI PMID:27029275 Cullin-RING ubiquitin E3 ligase regulation by the COP9 signa... | ACCEPT | Summary: Review of CRL regulation by CSN. The protein binding annotation reflects CSN-CRL interactions which are functionally important. Reason: The interaction between CSN and CRLs is central to CSN function in regulating ubiquitin ligase activity. Supporting Evidence: PMID:27029275 Cullin-RING ubiquitin E3 ligase regulation by the COP9 signalosome. |
| GO:0005515 protein binding | IPI PMID:27173435 An organelle-specific protein landscape identifies novel dis... | MARK AS OVER ANNOTATED | Summary: Organelle-specific protein landscape study. High-throughput interactome data. Reason: High-throughput study with generic annotation. Supporting Evidence: PMID:27173435 An organelle-specific protein landscape identifies novel diseases and molecular mechanisms. |
| GO:0005515 protein binding | IPI PMID:28514442 Architecture of the human interactome defines protein commun... | MARK AS OVER ANNOTATED | Summary: Human interactome architecture study. High-throughput interactome data. Reason: High-throughput study with generic annotation. Supporting Evidence: PMID:28514442 Architecture of the human interactome defines protein communities and disease networks. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | MARK AS OVER ANNOTATED | Summary: Human binary protein interactome reference map. High-throughput data. Reason: High-throughput study with generic annotation. Supporting Evidence: PMID:32296183 A reference map of the human binary protein interactome. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | MARK AS OVER ANNOTATED | Summary: Dual proteome-scale networks study. High-throughput interactome data. Reason: High-throughput study with generic annotation. Supporting Evidence: PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling of the human interactome. |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | MARK AS OVER ANNOTATED | Summary: Multimodal cell maps study. High-throughput data. Reason: High-throughput study with generic annotation. Supporting Evidence: PMID:40205054 Multimodal cell maps as a foundation for structural and functional genomics. |
| GO:0005654 nucleoplasm | IDA GO_REF:0000052 | ACCEPT | Summary: COPS8/CSN localizes to the nucleoplasm based on immunofluorescence data from HPA. This is consistent with the CSN's role in nuclear protein turnover regulation. Reason: Nucleoplasm localization is well-supported by immunofluorescence studies and consistent with CSN function in regulating nuclear CRL activity. Supporting Evidence: PMID:24421388 the complex is localized in the cytoplasm, nucleoplasm, and chromatin-bound fractions |
| GO:0005829 cytosol | IDA GO_REF:0000052 | ACCEPT | Summary: COPS8/CSN localizes to the cytosol based on HPA immunofluorescence data. This is consistent with multiple studies showing cytoplasmic CSN localization. Reason: Cytosolic localization is well-documented for CSN complex. Supporting Evidence: PMID:9535219 Immunofluorescence staining reveals that the new complex shows a subcellular distribution similar to that of the 26S proteasome. |
| GO:0005634 nucleus | IDA PMID:24421388 Dynamic regulation of the COP9 signalosome in response to DN... | ACCEPT | Summary: The CSN complex is localized in both nucleus and cytoplasm. PMID:24421388 provides direct experimental evidence for nuclear localization using biochemical and fluorescence microscopy analyses. Reason: Direct experimental evidence for nuclear localization of CSN complex including COPS8. Supporting Evidence: PMID:24421388 Through biochemical and fluorescence microscopy analyses, we determined that the complex is localized in the cytoplasm, nucleoplasm, and chromatin-bound fractions |
| GO:0005737 cytoplasm | IDA PMID:24421388 Dynamic regulation of the COP9 signalosome in response to DN... | ACCEPT | Summary: The CSN complex is localized in both nucleus and cytoplasm. PMID:24421388 provides direct experimental evidence for cytoplasmic localization. Reason: Direct experimental evidence for cytoplasmic localization of CSN complex. Supporting Evidence: PMID:24421388 the complex is localized in the cytoplasm, nucleoplasm, and chromatin-bound fractions |
| GO:0045116 protein neddylation | NAS PMID:24421388 Dynamic regulation of the COP9 signalosome in response to DN... | MODIFY | Summary: This annotation is problematic. The CSN complex is involved in protein DENEDDYLATION (removal of NEDD8), not neddylation (attachment of NEDD8). PMID:24421388 discusses CSN regulation of neddylation/deneddylation cycles but CSN is a deneddylase, not a neddylation enzyme. Reason: The CSN complex catalyzes deneddylation, not neddylation. While CSN participates in the neddylation/deneddylation cycle by removing NEDD8, it does not catalyze neddylation. The annotation should be 'protein deneddylation' or 'regulation of protein neddylation'. Proposed replacements: protein deneddylation Supporting Evidence: PMID:19141280 the catalytically active human complex, reconstituted in vitro, is composed of a single copy of each of the eight subunits |
| GO:2000434 regulation of protein neddylation | NAS PMID:24421388 Dynamic regulation of the COP9 signalosome in response to DN... | ACCEPT | Summary: The CSN regulates protein neddylation by catalyzing deneddylation, thus controlling the neddylation/deneddylation cycle of cullins. This annotation appropriately captures the regulatory role of CSN in the neddylation pathway. Reason: CSN regulates neddylation by deneddylating cullins, affecting CRL activity and the neddylation cycle. This is an accurate description of CSN function. Supporting Evidence: PMID:24421388 The COP9 signalosome (CSN) is an evolutionarily conserved protein complex that participates in the regulation of the ubiquitin/26S proteasome pathway by controlling the function of cullin-RING-ubiquitin ligases. |
| GO:0006468 protein phosphorylation | IDA PMID:9535219 A novel protein complex involved in signal transduction poss... | MODIFY | Summary: The CSN complex was found to have kinase activity that phosphorylates IkappaBalpha, p105, and c-Jun. However, this kinase activity is likely via association with CK2 and PKD kinases (as noted in UniProt), not intrinsic to CSN subunits including COPS8. COPS8 is a PCI-domain scaffold protein without kinase catalytic activity. Reason: COPS8 does not have intrinsic kinase activity. The phosphorylation activity of the CSN complex comes from associated kinases (CK2, PKD) rather than from CSN subunits themselves. A more accurate annotation would reflect the regulatory role rather than direct enzymatic activity. Proposed replacements: regulation of protein kinase activity Supporting Evidence: PMID:9535219 The isolated JAB1-containing particle has kinase activity that phosphorylates IkappaBalpha, the carboxy terminus of p105, and Ser63 and/or Ser73 of the amino-terminal activation domain of c-Jun. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8863721 | ACCEPT | Summary: Reactome annotation for CSN localization in cytosol based on NEDD8-related pathway. Consistent with experimental evidence. Reason: Cytosolic localization is well-documented. Reactome pathway annotations are reliable. Supporting Evidence: Reactome:R-HSA-8863721 NEDD8-STON binds TOR1 hexamer and COP9 complex |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8863723 | ACCEPT | Summary: Reactome annotation for CSN in cytosol involved in deneddylation. Reason: Cytosolic localization is correct and relevant to CSN function. Supporting Evidence: Reactome:R-HSA-8863723 COP9 and TOR1 deneddylate STON2 |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8956040 | ACCEPT | Summary: Reactome annotation for CSN deneddylation of cytosolic CRL complexes. Reason: Cytosolic localization is relevant to CSN function in regulating CRLs. Supporting Evidence: Reactome:R-HSA-8956040 COP9 signalosome deneddylates cytosolic CRL E3 ubiquitin ligase complexes |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5691006 | ACCEPT | Summary: Reactome annotation for CSN in nucleoplasm involved in DNA damage recognition in global genome nucleotide excision repair. Reason: Nucleoplasm localization is well-documented and relevant to CSN role in DNA damage response. Supporting Evidence: Reactome:R-HSA-5691006 XPC:RAD23:CETN2 and UV-DDB bind distorted dsDNA site |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-6781833 | ACCEPT | Summary: Reactome annotation for CSN in nucleoplasm involved in transcription-coupled nucleotide excision repair. Reason: Nucleoplasm localization is consistent with CSN role in DNA damage response. Supporting Evidence: Reactome:R-HSA-6781833 ERCC8 (CSA) binds stalled RNA Pol II |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-8956045 | ACCEPT | Summary: Reactome annotation for CSN deneddylation of nuclear CRL4 complex. Reason: Nucleoplasm localization is relevant to CSN function in regulating nuclear CRL complexes. Supporting Evidence: Reactome:R-HSA-8956045 COP9 signalosome deneddylates nuclear CRL4 E3 ubiquitin ligase complex |
| GO:0007250 activation of NF-kappaB-inducing kinase activity | IMP PMID:22992343 microRNA-146a inhibits G protein-coupled receptor-mediated a... | KEEP AS NON CORE | Summary: PMID:22992343 shows that COPS8 knockdown inhibits LPA-stimulated GPCR-mediated NF-kappaB activation. The study identifies COPS8 as a miR-146a target and shows that siRNA knockdown of COPS8 significantly inhibits LPA-induced NF-kappaB activity. This supports a role for COPS8 in NF-kappaB signaling. Reason: The annotation is supported by experimental evidence but represents a downstream effect of CSN function in regulating protein stability rather than a core molecular function of COPS8. The NF-kappaB regulation is likely mediated through CSN's role in CRL regulation affecting IkappaB stability. Supporting Evidence: PMID:22992343 siRNA knockdown of CARD10 and COPS8 expression significantly inhibited LPA-stimulated GPCR-mediated activation of NF-kappaB in SNU638 cells |
| GO:0008180 COP9 signalosome | IDA PMID:9535219 A novel protein complex involved in signal transduction poss... | ACCEPT | Summary: The original study identifying the human COP9 signalosome. COPS8 is identified as a subunit of the 450 kDa complex by mass spectrometry and biochemical analysis. Reason: Core function - fundamental paper establishing COPS8 as a CSN subunit. Supporting Evidence: PMID:9535219 A novel protein complex has been identified in human cells that has a molecular mass of approximately 450 kDa. It consists of at least eight different subunits |
| GO:0008285 negative regulation of cell population proliferation | IMP PMID:23689509 COP9 signalosome subunit Csn8 is involved in maintaining pro... | ACCEPT | Summary: PMID:23689509 shows that Csn8 hypomorphism (reduced CSN8 levels) leads to ACCELERATED cell growth, not negative regulation. The paper demonstrates that decreased CSN8 levels shorten G1 phase and increase proliferation. This annotation appears to be inverted - CSN8 normally restrains proliferation, so the annotation is technically correct but requires clarification. Reason: The study shows that normal CSN8 levels maintain proper G1 phase duration and prevent accelerated proliferation. Thus COPS8 does participate in negative regulation of proliferation under normal conditions. Supporting Evidence: PMID:23689509 A decreased level of Csn8, either in Csn8 hypomorphic MEFs or following siRNA-mediated knockdown in HeLa cells, accelerated cell growth rate. Csn8 hypomorphic MEFs exhibited a shortened G1 duration |
| GO:0048471 perinuclear region of cytoplasm | IDA PMID:9535219 A novel protein complex involved in signal transduction poss... | ACCEPT | Summary: The original CSN paper shows perinuclear localization by immunofluorescence, similar to the 26S proteasome distribution. Reason: Direct experimental evidence for perinuclear localization of the CSN complex. Supporting Evidence: PMID:9535219 Immunofluorescence staining reveals that the new complex shows a subcellular distribution similar to that of the 26S proteasome. |
| GO:0070062 extracellular exosome | HDA PMID:19056867 Large-scale proteomics and phosphoproteomics of urinary exos... | KEEP AS NON CORE | Summary: High-throughput proteomics study detecting COPS8 in urinary exosomes. This is likely a minor localization not representing core function. Reason: While COPS8 may be present in exosomes based on proteomics data, this does not represent a core functional localization. The primary sites of CSN function are nucleus and cytoplasm. Supporting Evidence: PMID:19056867 Large-scale proteomics and phosphoproteomics of urinary exosomes. |
| GO:0000338 protein deneddylation | IDA PMID:19141280 Symmetrical modularity of the COP9 signalosome complex sugge... | ACCEPT | Summary: The reconstituted CSN complex shows deneddylase activity. COPS8 is required for proper complex assembly and thus for deneddylation function, though the catalytic activity resides in CSN5. Reason: Core function. While COPS8 is not the catalytic subunit, it is essential for CSN holocomplex integrity and therefore for deneddylation activity. Supporting Evidence: PMID:19141280 the catalytically active human complex, reconstituted in vitro, is composed of a single copy of each of the eight subunits. By forming a total of 35 subcomplexes, we are able to build a comprehensive interaction map that shows two symmetrical modules, Csn1/2/3/8 and Csn4/5/6/7 |
| GO:0008180 COP9 signalosome | IDA PMID:18850735 Characterization of the human COP9 signalosome complex using... | ACCEPT | Summary: Affinity purification and mass spectrometry characterization confirming COPS8 as a CSN subunit with identification of post-translational modifications. Reason: Core function. Direct experimental evidence for COPS8 as a CSN complex subunit. Supporting Evidence: PMID:18850735 Mass spectrometric analysis of the purified CSN complex has revealed the identity of its composition as well as N-terminal modification and phosphorylation of the CSN subunits. |
| GO:0005634 nucleus | TAS PMID:8689678 The COP9 complex, a novel multisubunit nuclear regulator inv... | ACCEPT | Summary: Original study in Arabidopsis showing nuclear localization of the COP9 complex. Human CSN shows similar localization pattern. Reason: Nuclear localization is conserved for CSN complex across species. Supporting Evidence: PMID:8689678 The complex is acidic, binds heparin, and is localized within the nucleus. |
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Download this section (compressed HTML)Q: Does COPS8 have any function independent of the CSN complex?
Q: What are the specific structural contributions of COPS8 to CSN-substrate recognition?
Q: Are there tissue-specific or developmental-stage-specific roles for COPS8?
Experiment: Structural studies to define COPS8's specific contributions to CSN-CRL interactions
Experiment: Systematic analysis of CSN8 mutations on complex assembly and deneddylase activity
Experiment: Investigation of COPS8 phosphorylation (Ser-175) on CSN function
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