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Targeting of C‐Terminal (Tail)‐Anchored Proteins: Understanding how Cytoplasmic Activities are Anchored to Intracellular Membranes
Author(s) -
Wattenberg Binks,
Lithgow Trevor
Publication year - 2001
Publication title -
traffic
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.677
H-Index - 130
eISSN - 1600-0854
pISSN - 1398-9219
DOI - 10.1034/j.1600-0854.2001.20108.x
Subject(s) - biology , intracellular , microbiology and biotechnology , cytoplasm , cytosol , membrane protein , transport protein , integral membrane protein , c2 domain , peripheral membrane protein , organelle , protein sorting signals , protein targeting , membrane , biochemistry , peptide sequence , signal peptide , gene , enzyme
A class of integral membrane proteins, referred to as ‘tail‐anchored proteins’, are inserted into phospholipid bilayers via a single segment of hydrophobic amino acids at the C‐terminus, thereby displaying a large functional domain in the cytosol. This membrane attachment strategy allows eukaryotic cells to position a wide range of cytoplasmic activities close to the surface of an intracellular membrane. Tail‐anchored proteins often, but not always, demonstrate a selective distribution to specific intracellular organelles. This membrane‐specific distribution is required for the large number of targeting proteins that are tail‐anchored, but may or may not be critical for the numerous tail‐anchored pro‐apoptotic and anti‐apoptotic proteins of the Bcl‐2 family. Recent work has begun to address the mechanism for targeting tail‐anchored proteins to their resident membranes, but questions remain. What targeting signals determine each protein's intracellular location? Are there receptors for these signals and, if so, how do they function? What steps are required to integrate tail‐anchored proteins into the phospholipid bilayers? In this Traffic Interchange , we summarise what is known about tail‐anchored proteins, and outline the areas that are currently under study.