bMERB domains are bivalent Rab8 family effectors evolved by gene duplication
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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, Vol. 5, 23.08.2016.Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review
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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 -