Structures of Get3, Get4, and Get5 provide new models for TA membrane protein targeting

Peter J Simpson; Blanche Schwappach; Henrik G Dohlman; Rivka L Isaacson

doi:10.1016/j.str.2010.07.003

Structures of Get3, Get4, and Get5 provide new models for TA membrane protein targeting

Standard

Structures of Get3, Get4, and Get5 provide new models for TA membrane protein targeting. / Simpson, Peter J; Schwappach, Blanche; Dohlman, Henrik G; Isaacson, Rivka L.

In: STRUCTURE, Vol. 18, No. 8, 11.08.2010, p. 897-902.

Research output: SCORING: Contribution to journal › SCORING: Review article › Research

Harvard

Simpson, PJ, Schwappach, B, Dohlman, HG & Isaacson, RL 2010, 'Structures of Get3, Get4, and Get5 provide new models for TA membrane protein targeting', STRUCTURE, vol. 18, no. 8, pp. 897-902. https://doi.org/10.1016/j.str.2010.07.003

APA

Simpson, P. J., Schwappach, B., Dohlman, H. G., & Isaacson, R. L. (2010). Structures of Get3, Get4, and Get5 provide new models for TA membrane protein targeting. STRUCTURE, 18(8), 897-902. https://doi.org/10.1016/j.str.2010.07.003

Vancouver

Simpson PJ, Schwappach B, Dohlman HG, Isaacson RL. Structures of Get3, Get4, and Get5 provide new models for TA membrane protein targeting. STRUCTURE. 2010 Aug 11;18(8):897-902. https://doi.org/10.1016/j.str.2010.07.003

Bibtex

@article{1166b4ec8a08454092d7e1fdbf7ddb13,

title = "Structures of Get3, Get4, and Get5 provide new models for TA membrane protein targeting",

abstract = "The GET pathway, using several proteins (Gets 1-5 and probably Sgt2), posttranslationally conducts tail-anchored (TA) proteins to the endoplasmic reticulum (ER). At the ER, TA proteins are inserted into the lipid bilayer and then sorted and directed to their respective destinations in the secretory pathway. Until last year, there was no structural information on any of the GET components but now there are ten crystal structures of Get3 in a variety of nucleotide-bound states and conformations. The structures of Get4 and a portion of Get5 also emerged in 2010. This minireview provides a detailed comparison of the GET structures and discusses their mechanistic relevance to TA protein insertion. It also addresses the outstanding gaps in detailed molecular information on this system, including the structures of Get5, Sgt2, and the transmembrane complex comprising Get1 and Get2.",

keywords = "Adenosine Triphosphatases/chemistry, Carrier Proteins/chemistry, Endoplasmic Reticulum/metabolism, Guanine Nucleotide Exchange Factors/chemistry, Membrane Proteins, Models, Biological, Models, Molecular, Protein Transport, Saccharomyces cerevisiae Proteins/chemistry, Signal Transduction/physiology, Ubiquitin/chemistry",

author = "Simpson, {Peter J} and Blanche Schwappach and Dohlman, {Henrik G} and Isaacson, {Rivka L}",

year = "2010",

month = aug,

day = "11",

doi = "10.1016/j.str.2010.07.003",

language = "English",

volume = "18",

pages = "897--902",

journal = "STRUCTURE",

issn = "0969-2126",

publisher = "Cell Press",

number = "8",

}

RIS

TY - JOUR

T1 - Structures of Get3, Get4, and Get5 provide new models for TA membrane protein targeting

AU - Simpson, Peter J

AU - Schwappach, Blanche

AU - Dohlman, Henrik G

AU - Isaacson, Rivka L

PY - 2010/8/11

Y1 - 2010/8/11

N2 - The GET pathway, using several proteins (Gets 1-5 and probably Sgt2), posttranslationally conducts tail-anchored (TA) proteins to the endoplasmic reticulum (ER). At the ER, TA proteins are inserted into the lipid bilayer and then sorted and directed to their respective destinations in the secretory pathway. Until last year, there was no structural information on any of the GET components but now there are ten crystal structures of Get3 in a variety of nucleotide-bound states and conformations. The structures of Get4 and a portion of Get5 also emerged in 2010. This minireview provides a detailed comparison of the GET structures and discusses their mechanistic relevance to TA protein insertion. It also addresses the outstanding gaps in detailed molecular information on this system, including the structures of Get5, Sgt2, and the transmembrane complex comprising Get1 and Get2.

AB - The GET pathway, using several proteins (Gets 1-5 and probably Sgt2), posttranslationally conducts tail-anchored (TA) proteins to the endoplasmic reticulum (ER). At the ER, TA proteins are inserted into the lipid bilayer and then sorted and directed to their respective destinations in the secretory pathway. Until last year, there was no structural information on any of the GET components but now there are ten crystal structures of Get3 in a variety of nucleotide-bound states and conformations. The structures of Get4 and a portion of Get5 also emerged in 2010. This minireview provides a detailed comparison of the GET structures and discusses their mechanistic relevance to TA protein insertion. It also addresses the outstanding gaps in detailed molecular information on this system, including the structures of Get5, Sgt2, and the transmembrane complex comprising Get1 and Get2.

KW - Adenosine Triphosphatases/chemistry

KW - Carrier Proteins/chemistry

KW - Endoplasmic Reticulum/metabolism

KW - Guanine Nucleotide Exchange Factors/chemistry

KW - Membrane Proteins

KW - Models, Biological

KW - Models, Molecular

KW - Protein Transport

KW - Saccharomyces cerevisiae Proteins/chemistry

KW - Signal Transduction/physiology

KW - Ubiquitin/chemistry

U2 - 10.1016/j.str.2010.07.003

DO - 10.1016/j.str.2010.07.003

M3 - SCORING: Review article

C2 - 20696390

VL - 18

SP - 897

EP - 902

JO - STRUCTURE

JF - STRUCTURE

SN - 0969-2126

IS - 8

ER -