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bMERB domains are bivalent Rab8 family effectors evolved by gene duplication

Standard

bMERB domains are bivalent Rab8 family effectors evolved by gene duplication. / Rai, Amrita; Oprisko, Anastasia; Campos, Jeremy; Fu, Yangxue; Friese, Timon; Itzen, Aymelt; Goody, Roger S; Gazdag, Emerich Mihai.

in: ELIFE, Jahrgang 5, 23.08.2016.

Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung

Harvard

Rai, A, Oprisko, A, Campos, J, Fu, Y, Friese, T, Itzen, A, Goody, RS & Gazdag, EM 2016, 'bMERB domains are bivalent Rab8 family effectors evolved by gene duplication', ELIFE, Jg. 5. https://doi.org/10.7554/eLife.18675

APA

Rai, A., Oprisko, A., Campos, J., Fu, Y., Friese, T., Itzen, A., Goody, R. S., & Gazdag, E. M. (2016). bMERB domains are bivalent Rab8 family effectors evolved by gene duplication. ELIFE, 5. https://doi.org/10.7554/eLife.18675

Vancouver

Rai A, Oprisko A, Campos J, Fu Y, Friese T, Itzen A et al. bMERB domains are bivalent Rab8 family effectors evolved by gene duplication. ELIFE. 2016 Aug 23;5. https://doi.org/10.7554/eLife.18675

Bibtex

@article{fda69bc3a88e45c791723057186e2af0,
title = "bMERB domains are bivalent Rab8 family effectors evolved by gene duplication",
abstract = "In their active GTP-bound form, Rab proteins interact with proteins termed effector molecules. In this study, we have thoroughly characterized a Rab effector domain that is present in proteins of the Mical and EHBP families, both known to act in endosomal trafficking. Within our study, we show that these effectors display a preference for Rab8 family proteins (Rab8, 10, 13 and 15) and that some of the effector domains can bind two Rab proteins via separate binding sites. Structural analysis allowed us to explain the specificity towards Rab8 family members and the presence of two similar Rab binding sites that must have evolved via gene duplication. This study is the first to thoroughly characterize a Rab effector protein that contains two separate Rab binding sites within a single domain, allowing Micals and EHBPs to bind two Rabs simultaneously, thus suggesting previously unknown functions of these effector molecules in endosomal trafficking.",
keywords = "Adaptor Proteins, Signal Transducing, Carrier Proteins, Cytoskeletal Proteins, Evolution, Molecular, Gene Duplication, LIM Domain Proteins, Protein Domains, rab GTP-Binding Proteins, Journal Article, Research Support, Non-U.S. Gov't",
author = "Amrita Rai and Anastasia Oprisko and Jeremy Campos and Yangxue Fu and Timon Friese and Aymelt Itzen and Goody, {Roger S} and Gazdag, {Emerich Mihai}",
year = "2016",
month = aug,
day = "23",
doi = "10.7554/eLife.18675",
language = "English",
volume = "5",
journal = "ELIFE",
issn = "2050-084X",
publisher = "eLife Sciences Publications",

}

RIS

TY - JOUR

T1 - bMERB domains are bivalent Rab8 family effectors evolved by gene duplication

AU - Rai, Amrita

AU - Oprisko, Anastasia

AU - Campos, Jeremy

AU - Fu, Yangxue

AU - Friese, Timon

AU - Itzen, Aymelt

AU - Goody, Roger S

AU - Gazdag, Emerich Mihai

PY - 2016/8/23

Y1 - 2016/8/23

N2 - In their active GTP-bound form, Rab proteins interact with proteins termed effector molecules. In this study, we have thoroughly characterized a Rab effector domain that is present in proteins of the Mical and EHBP families, both known to act in endosomal trafficking. Within our study, we show that these effectors display a preference for Rab8 family proteins (Rab8, 10, 13 and 15) and that some of the effector domains can bind two Rab proteins via separate binding sites. Structural analysis allowed us to explain the specificity towards Rab8 family members and the presence of two similar Rab binding sites that must have evolved via gene duplication. This study is the first to thoroughly characterize a Rab effector protein that contains two separate Rab binding sites within a single domain, allowing Micals and EHBPs to bind two Rabs simultaneously, thus suggesting previously unknown functions of these effector molecules in endosomal trafficking.

AB - In their active GTP-bound form, Rab proteins interact with proteins termed effector molecules. In this study, we have thoroughly characterized a Rab effector domain that is present in proteins of the Mical and EHBP families, both known to act in endosomal trafficking. Within our study, we show that these effectors display a preference for Rab8 family proteins (Rab8, 10, 13 and 15) and that some of the effector domains can bind two Rab proteins via separate binding sites. Structural analysis allowed us to explain the specificity towards Rab8 family members and the presence of two similar Rab binding sites that must have evolved via gene duplication. This study is the first to thoroughly characterize a Rab effector protein that contains two separate Rab binding sites within a single domain, allowing Micals and EHBPs to bind two Rabs simultaneously, thus suggesting previously unknown functions of these effector molecules in endosomal trafficking.

KW - Adaptor Proteins, Signal Transducing

KW - Carrier Proteins

KW - Cytoskeletal Proteins

KW - Evolution, Molecular

KW - Gene Duplication

KW - LIM Domain Proteins

KW - Protein Domains

KW - rab GTP-Binding Proteins

KW - Journal Article

KW - Research Support, Non-U.S. Gov't

U2 - 10.7554/eLife.18675

DO - 10.7554/eLife.18675

M3 - SCORING: Journal article

C2 - 27552051

VL - 5

JO - ELIFE

JF - ELIFE

SN - 2050-084X

ER -