The tale of tail-anchored proteins: coming from the cytosol and looking for a membrane.
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.
Borgese
Nica
N
Consiglio Nazionale delle Ricerche Institute for Neuroscience, Cellular and Molecular Pharmacology Section, via Vanvitelli 32, 20129 Milano, Italy. n.borgese@in.cnr.it
Colombo
Sara
S
Pedrazzini
Emanuela
E
D000818:Animals; D002462:Cell Membrane / Q000378:metabolism*; D003600:Cytosol / Q000378:metabolism; D005057:Eukaryotic Cells / Q000378:metabolism*; D006801:Humans; D007425:Intracellular Membranes / Q000378:metabolism; D008565:Membrane Proteins / Q000378:metabolism*; D015394:Molecular Structure; D011499:Protein Processing, Post-Translational / Q000502:physiology; D017434:Protein Structure, Tertiary / Q000502:physiology
D008565:Membrane Proteins