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J Biol Chem, Vol. 273, Issue 21, 12740-12745, May 22, 1998
From the Centro de Biología Molecular "Severo Ochoa,"
Universidad Autónoma de Madrid, Consejo Superior de
Investigaciones Científicas, Cantoblanco,
28049-Madrid, Spain
The MAL (VIP17, MVP17) proteolipid, an integral
membrane protein with specific residence in glycolipid-enriched
membrane (GEM) microdomains, has been recently proposed as a component
of the protein machinery for GEM vesiculation. In this work, we have searched the COOH terminus of MAL for sorting determinants responsible for targeting to GEMs. This has allowed the identification of the
sequence Leu-Ile-Arg-Trp (LIRW) as necessary for the access of MAL to
GEMs. This motif requires at least one additional amino acid at its
COOH end for full effectiveness. The arginine within the LIRW motif is
the most crucial residue for targeting to GEMs, tryptophan replacement
affects targeting to a lesser extent, and the leucine-isoleucine pair
tolerates substitution by valine, but not by alanine, without effect on
targeting. Pulse-chase experiments indicate that the LIRW tetrapeptide
is required for access to GEMs early after MAL biosynthesis.
Interestingly, the loss of the capacity of the MAL protein to be
incorporated into GEMs correlated with the loss of its response to
brefeldin A treatment. This is the first identification of a
juxtamembrane peptide motif required for incorporation of an integral
membrane protein into GEMs.
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