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COMMD Proteins, a Novel Family of Structural and Functional Homologs of MURR1
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The ten members of the COMMD protein family readily form heterodimers both in vitro and in cells through their conserved C-terminal COMM domains.
“The ten members of the COMMD protein family are known to readily form heterodimers both in vitro and in cells through their conserved C-terminal COMM domains15,17.”
From Structural organization of the retriever–CCC endosomal recycling complex (2024) · cites this paper as [17]
The COMMD1 interaction results (Fig. 3A; page unavailable) show that all ten COMMD proteins can associate with COMMD1 in assays using proteins expressed in 293 cells. The COMM-domain mapping results (Fig. 3C–D; page unavailable) show that COMMD1’s C-terminal domain mediates its interactions with COMMD1 and COMMD3. The paper does not establish that all ten readily form heterodimers with one another, or demonstrate such dimers both in vitro and in cells. (LLM, conf=0.87)
Experimental — accuracy not yet measuredCCC is required for retromer- and retriever-dependent protein trafficking.
“the CCC protein complex, which consists of CCDC22, CCDC93, and any of the 10 COMMD proteins, is required for retromer- and retriever-dependent protein trafficking27–32”
From Endosomal PI(3)P regulation by the COMMD/CCDC22/CCDC93 (CCC) complex controls membrane protein recycling (2019) · cites this paper as [28]
The section on COMMD1 interactions reports ten COMMD proteins and shows that COMMD1 can associate with the other family members (page not available). It does not establish that they form a CCC complex with CCDC22 and CCDC93, or that CCC is required for retromer- or retriever-dependent trafficking. Thus it supports only the COMMD-family portion of the cited sentence, not the trafficking claim. (LLM, conf=0.82)
Experimental — accuracy not yet measuredThe CCC protein complex consists of CCDC22, CCDC93, and any of the 10 COMMD proteins.
“the CCC protein complex, which consists of CCDC22, CCDC93, and any of the 10 COMMD proteins”
From Endosomal PI(3)P regulation by the COMMD/CCDC22/CCDC93 (CCC) complex controls membrane protein recycling (2019) · cites this paper as [28]
The “COMMD1 Can Associate with Other COMMD Proteins” section identifies 10 COMMD proteins and reports that COMMD1 interacts with the others (page unavailable). It does not identify a CCC complex or establish that CCDC22 and CCDC93 form a complex with any of those proteins; searches for those names and the CCC complex found no such passage. (LLM, conf=0.88)
Experimental — accuracy not yet measuredCOMMD proteins possess a C-terminal COMM domain approximately 70-80 residues in length and an α-helical N-terminal (HN) domain.
“The COMMD proteins possess a C-terminal COMM domain approximately 70–80 residues in length, as well as an α-helical N-terminal (HN) domain.41,42”
From Structure of the endosomal Commander complex linked to Ritscher-Schinzel syndrome (2023) · cites this paper as [41]
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Metadata
- Authors
- Burstein, E., Hoberg, J. E., Wilkinson, A. S., Rumble, J. M., Csomos, R. A., Komarck, C. M., Maine, G. N., Wilkinson, J. C., Mayo, M. W., & Duckett, C. S.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2005-06
- Volume
- 280
- Issue
- 23
- Pages
- 22222-22232
- ISSN
- 0021-9258
- Cited by
- 258
- References
- 3
- Language
- en
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