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Structural characterization of the Get4/Get5 complex and its interaction with Get3

Chartron, Justin W. and Suloway, Christian J. M. and Zaslaver, Ma’ayan and Clemons, William M., Jr. (2010) Structural characterization of the Get4/Get5 complex and its interaction with Get3. Proceedings of the National Academy of Sciences of the United States of America, 107 (27). pp. 12127-12132. ISSN 0027-8424. PMCID PMC2901463. https://resolver.caltech.edu/CaltechAUTHORS:20100803-091147006

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Abstract

The recently elucidated Get proteins are responsible for the targeted delivery of the majority of tail-anchored (TA) proteins to the endoplasmic reticulum. Get4 and Get5 have been identified in the early steps of the pathway mediating TA substrate delivery to the cytoplasmic targeting factor Get3. Here we report a crystal structure of Get4 and an N-terminal fragment of Get5 from Saccharomyces cerevisae. We show Get4 and Get5 (Get4/5) form an intimate complex that exists as a dimer (two copies of Get4/5) mediated by the C-terminus of Get5. We further demonstrate that Get3 specifically binds to a conserved surface on Get4 in a nucleotide dependent manner. This work provides further evidence for a model in which Get4/5 operates upstream of Get3 and mediates the specific delivery of a TA substrate.


Item Type:Article
Related URLs:
URLURL TypeDescription
http://dx.doi.org/10.1073/pnas.1006036107 DOIArticle
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2901463/PubMed CentralArticle
http://www.pnas.org/lookup/suppl/doi:10.1073/pnas.1006036107/-/DCSupplementalPublisherSupporting Information
ORCID:
AuthorORCID
Clemons, William M., Jr.0000-0002-0021-889X
Additional Information:© 2010 by the National Academy of Sciences. Freely available online through the PNAS open access option. Communicated by Douglas C. Rees, Caltech/HHMI, Pasadena, CA, May 4, 2010 (received for review March 8, 2010). We thank J. Howard, A. Müller, and A. Palazzo for discussion and critical comments on the manuscript, and T. Walton for help with MALS. We thank Gordon and Betty Moore for support of the Molecular Observatory at Caltech. All data collection was performed at beamline 9-2 and 11-1 at SSRL. Operations at Stanford Synchrotron Radiation Laboratory are supported by the US Department of Energy and the National Institutes of Health. W.M.C. is supported by the Searle Scholar program and a Burroughs– Wellcome Fund Career Award for the Biological Sciences. Author contributions: J.W.C. and W.M.C. designed research; J.W.C. performed research; J.W.C., C.J.M.S., and M.Z. contributed new reagents/analytic tools; J.W.C. and W.M.C. analyzed data; and J.W.C., C.J.M.S., and W.M.C. wrote the paper.
Funders:
Funding AgencyGrant Number
Caltech Molecular ObservatoryUNSPECIFIED
Department of Energy (DOE)UNSPECIFIED
NIHUNSPECIFIED
Searle Scholars ProgramUNSPECIFIED
Burroughs-Wellcome FundUNSPECIFIED
Subject Keywords:crystallography; Get pathway; Mdy2; Ubl4a; tail-anchor
Issue or Number:27
PubMed Central ID:PMC2901463
Record Number:CaltechAUTHORS:20100803-091147006
Persistent URL:https://resolver.caltech.edu/CaltechAUTHORS:20100803-091147006
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:19252
Collection:CaltechAUTHORS
Deposited By: Tony Diaz
Deposited On:03 Aug 2010 20:39
Last Modified:03 Oct 2019 01:54

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