Journal
JOURNAL OF CELL BIOLOGY
Volume 161, Issue 6, Pages 1013-1019Publisher
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.200303069
Keywords
endoplasmic reticulum; membrane traffic; mitochondrial outer membrane; protein targeting and translocation; transmembrane domain
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A group of integral membrane proteins, known as C-tail anchored, is defined by the presence of a cytosolic NH2-terminal domain that is anchored to the phospholipid bilayer by a single segment of hydrophobic amino acids close to the COOH terminus. The mode of insertion into membranes of these proteins, many of which play key roles in fundamental intracellular processes, is obligatorily posttranslational, is highly specific, and may be subject to regulatory processes that modulate the protein's function. Although recent work has elucidated structural features in the tail region that determine selection of the correct target membrane, the molecular machinery involved in interpreting this information, and in modulating tail-anchored protein localization, has not been identified yet.
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