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Structural insights into the architecture and membrane interactions of the conserved COMMD proteins

Healy, Michael D, Hospenthal, Manuela K, Hall, Ryan J, Chandra, Mintu, Chilton, Molly, Tillu, Vikas, Chen, Kai-En, Celligoi, Dion J, McDonald, Fiona J, Cullen, Peter J, Lott, J Shaun, Collins, Brett M, Ghai, Rajesh·2018·eLife
DOI 10.7554/elife.35898PMC PMC6089597
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Abstract

The COMMD proteins are a conserved family of proteins with central roles in intracellular membrane trafficking and transcription. They form oligomeric complexes with each other and act as components of a larger assembly called the CCC complex, which is localized to endosomal compartments and mediates the transport of several transmembrane cargos. How these complexes are formed however is completely unknown. Here, we have systematically characterised the interactions between human COMMD proteins, and determined structures of COMMD proteins using X-ray crystallography and X-ray scattering to provide insights into the underlying mechanisms of homo- and heteromeric assembly. All COMMD proteins possess an α-helical N-terminal domain, and a highly conserved C-terminal domain that forms a tightly interlocked dimeric structure responsible for COMMD-COMMD interactions. The COMM domains also bind directly to components of CCC and mediate non-specific membrane association. Overall these studies show that COMMD proteins function as obligatory dimers with conserved domain architectures.

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Crossref · 10.7554/elife.35898

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  • Higher order COMMD hexamers may be possible through additional interactions via their shared helical N-terminal domains.

    “these studies suggest that higher order COMMD hexamers may be possible through additional interactions via their shared helical N-terminal domains.”

    From Endosomal PI(3)P regulation by the COMMD/CCDC22/CCDC93 (CCC) complex controls membrane protein recycling (2019) · cites this paper as [68]

    The Discussion speculates that COMMD N-terminal domains may contribute to higher-order assemblies and notes that related proteins form hexamers through N-terminal interactions. It does not specifically propose a hexameric stoichiometry for COMMD proteins; it says the stoichiometries of their larger complexes remain undetermined. No page number is available in our copy. (LLM, conf=0.85)

    Experimental — accuracy not yet measured

  • The COMM domain has high sequence similarity across the ten COMMD proteins and is composed of three anti-parallel β-strands and a C-terminal α-helix.

    “The COMM domain has high sequence similarity across the ten proteins and is composed of three anti-parallel β-strands, β1-β3, and a C-terminal α-helix α7.42”

    From Structure of the endosomal Commander complex linked to Ritscher-Schinzel syndrome (2023) · cites this paper as [42]

    The Results section on the Commd9 crystal structure describes each COMM-domain monomer as an N-terminal three-stranded β-sheet capped by an α-helix. The Results section on the conserved dimerization interface reports that COMM domains are highly conserved across the COMMD family. Our copy does not explicitly establish that the three β-strands are antiparallel. (LLM, conf=0.82)

    Experimental — accuracy not yet measured

  • The HN domain has a conserved globular structure of six α-helices α1-α6.

    “The HN domain, while relatively divergent in sequence, has a conserved globular structure of six α-helices α1-α6.42,43”

    From Structure of the endosomal Commander complex linked to Ritscher-Schinzel syndrome (2023) · cites this paper as [42]

    The Results section, “Crystal structure of the Commd9 N-terminal HN domain,” describes Commd9’s HN domain as a globular six-helix bundle and says HN domains are broadly conserved despite sequence variation. But it also states that Commd1 lacks α1 and shares only helices α2–α6, so six helices are not established as a conserved feature of every HN domain. (LLM, conf=0.89)

    Experimental — accuracy not yet measured

  • The interfaces are centered around Trp157 of COMMD5 and Trp139 of COMMD7, which are strictly conserved across all homologues and species of every COMMD protein.

    “For clarity, we describe these two interfaces as centered around Trp157 of COMMD5 and Trp139 of COMMD7 (Figures 3F and 3H), as these Trp residues are the only residues that are strictly conserved across all homologues and species of every COMMD protein.42”

    From Structure of the endosomal Commander complex linked to Ritscher-Schinzel syndrome (2023) · cites this paper as [42]

    The Results section on CCDC22 and CCDC93 binding says that Trp128 of COMMD9 is strictly conserved across the COMMD family, supporting conservation of a corresponding tryptophan. It does not establish that Trp157 of COMMD5 and Trp139 of COMMD7 are the only residues strictly conserved across every homologue and species. The description of the interfaces as ‘centered around’ those residues is the citing authors’ own framing. (LLM, conf=0.82)

    Experimental — accuracy not yet measured

  • Apart from COMMD9 and VPS29, the structure of Commander is almost completely uncharacterized, and the stoichiometry of the different subunits remains unclear.

    “Apart from COMMD942 and VPS29,44,45,46,47,48,49,50,51 the structure of Commander is almost completely uncharacterized, and the stoichiometry of the different subunits remain unclear.”

    From Structure of the endosomal Commander complex linked to Ritscher-Schinzel syndrome (2023) · cites this paper as [42]

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Metadata

Authors
Healy, M. D., Hospenthal, M. K., Hall, R. J., Chandra, M., Chilton, M., Tillu, V., Chen, K.-E., Celligoi, D. J., McDonald, F. J., Cullen, P. J., Lott, J. S., Collins, B. M., & Ghai, R.
Venue
eLife
Publisher
eLife Sciences Publications, Ltd
Published
2018-08-01
Volume
7
ISSN
2050-084X
DOI
10.7554/elife.35898
PMC
PMC6089597
Cited by
50
References
3
Language
en
Licence
Funders
  • Royal Society of New Zealand (Marsden fund: UOO-04-09)
  • Wellcome (089928, 104568)
  • Medical Research Council (MR/K018299/1, MR/P018807/1)
  • Australian Research Council (DP160101743)
  • National Health and Medical Research Council (APP1058734, APP1061574, 1097185)
  • University of Queensland (Early career researcher grant: 2016003796)

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