Biogenesis of tail-anchored proteins (Articolo in rivista)

Type
Label
  • Biogenesis of tail-anchored proteins (Articolo in rivista) (literal)
Anno
  • 2003-01-01T00:00:00+01:00 (literal)
Alternative label
  • Borgese N, Brambillasca S, Soffientini P, Yabal M, Makarow M. (2003)
    Biogenesis of tail-anchored proteins
    in Biochemical Society transactions
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Borgese N, Brambillasca S, Soffientini P, Yabal M, Makarow M. (literal)
Pagina inizio
  • 1238 (literal)
Pagina fine
  • 1242 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 31 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#note
  • IF 2,21 (literal)
Note
  • ISI Web of Science (WOS) (literal)
Titolo
  • Biogenesis of tail-anchored proteins (literal)
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. (literal)
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