The Ways of Tails: the GET Pathway and more

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The Ways of Tails: the GET Pathway and more : the GET Pathway and more. / Borgese, Nica; Coy-Vergara, Javier; Colombo, Sara Francesca; Schwappach, Blanche.

in: The protein journal, Jahrgang 38, Nr. 3, 06.2019, S. 289-305.

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@article{462bf4c2c0e94e74a7a1dbb613255f63,
title = "The Ways of Tails: the GET Pathway and more: the GET Pathway and more",
abstract = "Due to their topology tail-anchored (TA) proteins must target to the membrane independently of the co-translational route defined by the signal sequence recognition particle (SRP), its receptor and the translocon Sec61. More than a decade of work has extensively characterized a highly conserved pathway, the yeast GET or mammalian TRC40 pathway, which is capable of countering the biogenetic challenge posed by the C-terminal TA anchor. In this review we briefly summarize current models of this targeting route and focus on emerging aspects such as the intricate interplay with the proteostatic network of cells and with other targeting pathways. Importantly, we consider the lessons provided by the in vivo analysis of the pathway in different model organisms and by the consideration of its full client spectrum in more recent studies. This analysis of the state of the field highlights directions in which the current models may be experimentally probed and conceptually extended.",
keywords = "Animals, Cell Membrane/metabolism, Humans, Membrane Proteins/chemistry, Mice, Protein Processing, Post-Translational, Protein Transport, Saccharomyces cerevisiae/metabolism, Saccharomyces cerevisiae Proteins/metabolism, Signal Recognition Particle/chemistry",
author = "Nica Borgese and Javier Coy-Vergara and Colombo, {Sara Francesca} and Blanche Schwappach",
year = "2019",
month = jun,
doi = "10.1007/s10930-019-09845-4",
language = "English",
volume = "38",
pages = "289--305",
journal = "PROTEIN J",
issn = "1572-3887",
publisher = "Springer New York",
number = "3",

}

RIS

TY - JOUR

T1 - The Ways of Tails: the GET Pathway and more

T2 - the GET Pathway and more

AU - Borgese, Nica

AU - Coy-Vergara, Javier

AU - Colombo, Sara Francesca

AU - Schwappach, Blanche

PY - 2019/6

Y1 - 2019/6

N2 - Due to their topology tail-anchored (TA) proteins must target to the membrane independently of the co-translational route defined by the signal sequence recognition particle (SRP), its receptor and the translocon Sec61. More than a decade of work has extensively characterized a highly conserved pathway, the yeast GET or mammalian TRC40 pathway, which is capable of countering the biogenetic challenge posed by the C-terminal TA anchor. In this review we briefly summarize current models of this targeting route and focus on emerging aspects such as the intricate interplay with the proteostatic network of cells and with other targeting pathways. Importantly, we consider the lessons provided by the in vivo analysis of the pathway in different model organisms and by the consideration of its full client spectrum in more recent studies. This analysis of the state of the field highlights directions in which the current models may be experimentally probed and conceptually extended.

AB - Due to their topology tail-anchored (TA) proteins must target to the membrane independently of the co-translational route defined by the signal sequence recognition particle (SRP), its receptor and the translocon Sec61. More than a decade of work has extensively characterized a highly conserved pathway, the yeast GET or mammalian TRC40 pathway, which is capable of countering the biogenetic challenge posed by the C-terminal TA anchor. In this review we briefly summarize current models of this targeting route and focus on emerging aspects such as the intricate interplay with the proteostatic network of cells and with other targeting pathways. Importantly, we consider the lessons provided by the in vivo analysis of the pathway in different model organisms and by the consideration of its full client spectrum in more recent studies. This analysis of the state of the field highlights directions in which the current models may be experimentally probed and conceptually extended.

KW - Animals

KW - Cell Membrane/metabolism

KW - Humans

KW - Membrane Proteins/chemistry

KW - Mice

KW - Protein Processing, Post-Translational

KW - Protein Transport

KW - Saccharomyces cerevisiae/metabolism

KW - Saccharomyces cerevisiae Proteins/metabolism

KW - Signal Recognition Particle/chemistry

U2 - 10.1007/s10930-019-09845-4

DO - 10.1007/s10930-019-09845-4

M3 - SCORING: Review article

C2 - 31203484

VL - 38

SP - 289

EP - 305

JO - PROTEIN J

JF - PROTEIN J

SN - 1572-3887

IS - 3

ER -