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Biochem Soc Trans. 2003 Dec;31(Pt 6):1238-42.

Biogenesis of tail-anchored proteins.

Author information

1
Consiglio Nazionale delle Ricerche Institute for Neuroscience, Cellular and Molecular Pharmacology Section, University of Milan, via Vanvitelli 32, 20129 Milan, Italy. n.borgese@in.cnr.it

Abstract

A group of integral membrane proteins, known as C-tail anchored, is defined by the presence of a cytosolic N-terminal domain that is anchored to the phospholipid bilayer by a single segment of hydrophobic amino acids close to the C-terminus. The mode of insertion into membranes of these proteins, many of which play key roles in fundamental intracellular processes, is obligatorily post-translational, is highly specific and may be subject to regulatory processes that modulate the protein's function. Recent work has demonstrated that tail-anchored proteins translocate their C-termini across the endoplasmic reticulum membrane by a mechanism different from that used for Sec61-dependent post-translational signal-peptide-driven translocation. Here we summarize recent results on the insertion of tail-anchored proteins and discuss possible mechanisms that could be involved.

PMID:
14641033
DOI:
10.1042/bst0311238
[Indexed for MEDLINE]

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