Structural Basis for Budding by the ESCRT-III Factor CHMP3

Muzioł, Tadeusz; Pineda‐Molina, Estela; Ravelli, Raimond B. G.; Zamborlini, Alessia; Usami, Yoshiko; Göttlinger, Heinrich G.; Weissenhorn, Winfríed

doi:10.1016/j.devcel.2006.03.013

Cited by 223 publications

(339 citation statements)

References 47 publications

(94 reference statements)

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“…prevents oligomerization on the membrane surface (38). Furthermore, Arf and Sar GTPases release an N-terminal helix upon GTP binding that inserts into the membrane and induces membrane remodeling (39,40).…”

Section: Discussionmentioning

confidence: 99%

Structural basis of oligomerization in septin-like GTPase of immunity-associated protein 2 (GIMAP2)

Schwefel

Fröhlich²,

Eichhorst³

et al. 2010

Proc. Natl. Acad. Sci. U.S.A.

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GTPases of immunity-associated proteins (GIMAPs) are a distinctive family of GTPases, which control apoptosis in lymphocytes and play a central role in lymphocyte maturation and lymphocyte-associated diseases. To explore their function and mechanism, we determined crystal structures of a representative member, GIMAP2, in different nucleotide-loading and oligomerization states. Nucleotide-free and GDP-bound GIMAP2 were monomeric and revealed a guanine nucleotide-binding domain of the TRAFAC (translation factor associated) class with a unique amphipathic helix α7 packing against switch II. In the absence of α7 and the presence of GTP, GIMAP2 oligomerized via two distinct interfaces in the crystal. GTP-induced stabilization of switch I mediates dimerization across the nucleotide-binding site, which also involves the GIMAP specificity motif and the nucleotide base. Structural rearrangements in switch II appear to induce the release of α7 allowing oligomerization to proceed via a second interface. The unique architecture of the linear oligomer was confirmed by mutagenesis. Furthermore, we showed a function for the GIMAP2 oligomer at the surface of lipid droplets. Although earlier studies indicated that GIMAPs are related to the septins, the current structure also revealed a strikingly similar nucleotide coordination and dimerization mode as in the dynamin GTPase. Based on this, we reexamined the relationships of the septin-and dynamin-like GTPases and demonstrate that these are likely to have emerged from a common membrane-associated dimerizing ancestor. This ancestral property appears to be critical for the role of GIMAPs as nucleotide-regulated scaffolds on intracellular membranes. G protein | protein structure

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Section: Discussionmentioning

confidence: 99%

Structural basis of oligomerization in septin-like GTPase of immunity-associated protein 2 (GIMAP2)

Schwefel

Fröhlich²,

Eichhorst³

et al. 2010

Proc. Natl. Acad. Sci. U.S.A.

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“…Humans have 10 ESCRT-III-related proteins, denoted CHMP, that can be classified into six families corresponding to the six yeast proteins (2,3). ESCRT-III-related proteins share a similar structural organization, as determined from structural studies of the human Vps24p orthologue CHMP3 (33,34). This structural organization involves a basic N-terminal domain formed by four helices and a C-terminal acidic region that, in certain ESCRT-III-related proteins, mediates recruitment of ESCRT-III interactors containing one or more MIT domains (see Ref.…”

mentioning

confidence: 93%

Physiological Involvement in pH Signaling of Vps24-mediated Recruitment of Aspergillus PalB Cysteine Protease to ESCRT-III

Rodríguez-Galán

Galindo

Hervás-Aguilar

et al. 2009

Journal of Biological Chemistry

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“…The three-dimensional structure has been solved for some ESCRT-III proteins (Muziol et al 2006;Bajorek et al 2009). The basic structure consists of six a-helices.…”

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confidence: 99%

Evidence for a Nonendosomal Function of the Saccharomyces cerevisiae ESCRT-III-Like Protein Chm7

et al. 2015

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Endosomal sorting complex required for transport (ESCRT) proteins are involved in a number of cellular processes, such as endosomal protein sorting, HIV budding, cytokinesis, plasma membrane repair, and resealing of the nuclear envelope during mitosis. Here we explored the function of a noncanonical member of the ESCRT-III protein family, the Saccharomyces cerevisiae ortholog of human CHMP7. Very little is known about this protein. In silico analysis predicted that Chm7 (yeast ORF YJL049w) is a fusion of an ESCRT-II and ESCRT-III-like domain, which would suggest a role in endosomal protein sorting. However, our data argue against a role of Chm7 in endosomal protein sorting. The turnover of the endocytic cargo protein Ste6 and the vacuolar protein sorting of carboxypeptidase S (CPS) were not affected by CHM7 deletion, and Chm7 also responded very differently to a loss in Vps4 function compared to a canonical ESCRT-III protein. Our data indicate that the Chm7 function could be connected to the endoplasmic reticulum (ER). In line with a function at the ER, we observed a strong negative genetic interaction between the deletion of a gene function (APQ12) implicated in nuclear pore complex assembly and messenger RNA (mRNA) export and the CHM7 deletion. The patterns of genetic interactions between the APQ12 deletion and deletions of ESCRT-III genes, two-hybrid interactions, and the specific localization of mCherry fusion proteins are consistent with the notion that Chm7 performs a novel function at the ER as part of an alternative ESCRT-III complex.

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Structural Basis for Budding by the ESCRT-III Factor CHMP3

Cited by 223 publications

References 47 publications

Structural basis of oligomerization in septin-like GTPase of immunity-associated protein 2 (GIMAP2)

Structural basis of oligomerization in septin-like GTPase of immunity-associated protein 2 (GIMAP2)

Physiological Involvement in pH Signaling of Vps24-mediated Recruitment of Aspergillus PalB Cysteine Protease to ESCRT-III

Evidence for a Nonendosomal Function of the Saccharomyces cerevisiae ESCRT-III-Like Protein Chm7

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