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Structure of membrane tethers and their role in fusion
Author(s) -
Ungermann Christian,
Kümmel Daniel
Publication year - 2019
Publication title -
traffic
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.677
H-Index - 130
eISSN - 1600-0854
pISSN - 1398-9219
DOI - 10.1111/tra.12655
Subject(s) - rab , tethering , vesicular transport proteins , biology , microbiology and biotechnology , gtpase , lipid bilayer fusion , vesicle , vesicular transport protein , compartment (ship) , transport protein , copii , endosome , membrane , secretory pathway , golgi apparatus , biochemistry , oceanography , vacuolar protein sorting , endoplasmic reticulum , geology , intracellular
Vesicular transport between different membrane compartments is a key process in cell biology required for the exchange of material and information. The complex machinery that executes the formation and delivery of transport vesicles has been intensively studied and yielded a comprehensive view of the molecular principles that underlie the budding and fusion process. Tethering also represents an essential step in each trafficking pathway. It is mediated by Rab GTPases in concert with so‐called tethering factors, which constitute a structurally diverse family of proteins that share a similar role in promoting vesicular transport. By simultaneously binding to proteins and/or lipids on incoming vesicles and the target compartment, tethers are thought to bridge donor and acceptor membrane. They thus provide specificity while also promoting fusion. However, how tethering works at a mechanistic level is still elusive. We here discuss the recent advances in the structural and biochemical characterization of tethering complexes that provide novel insight on how these factors might contribute the efficiency of fusion.