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Titolo:
PALMITOYLATION OF P59(FYN) IS REVERSIBLE AND SUFFICIENT FOR PLASMA-MEMBRANE ASSOCIATION
Autore:
WOLVEN A; OKAMURA H; ROSENBLATT Y; RESH MD;
Indirizzi:
MEM SLOAN KETTERING CANC CTR,CELL BIOL & GENET PROGRAM,1275 YORK AVE,BOX 143 NEW YORK NY 10021 MEM SLOAN KETTERING CANC CTR,CELL BIOL & GENET PROGRAM NEW YORK NY 10021 CORNELL UNIV,GRAD SCH MED SCI,PROGRAM MOL BIOL NEW YORK NY 10021 CORNELL UNIV,GRAD SCH MED SCI,PROGRAM CELL BIOL & GENET & BIOCHEM NEWYORK NY 10021
Titolo Testata:
Molecular biology of the cell
fascicolo: 6, volume: 8, anno: 1997,
pagine: 1159 - 1173
SICI:
1059-1524(1997)8:6<1159:POPIRA>2.0.ZU;2-J
Fonte:
ISI
Lingua:
ENG
Soggetto:
PROTEIN-TYROSINE KINASES; PHOSPHORYLATED IG-ALPHA; CELL ANTIGEN RECEPTOR; SRC FAMILY; SIGNAL-TRANSDUCTION; POLYBASIC DOMAIN; MYRISTOYLATED PROTEINS; TRANSFORMED-CELLS; ANCHORED PROTEINS; FATTY-ACIDS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
58
Recensione:
Indirizzi per estratti:
Citazione:
A. Wolven et al., "PALMITOYLATION OF P59(FYN) IS REVERSIBLE AND SUFFICIENT FOR PLASMA-MEMBRANE ASSOCIATION", Molecular biology of the cell, 8(6), 1997, pp. 1159-1173

Abstract

Members of the Src family of protein tyrosine kinases are localized to subspecialized regions of the plasma membrane. Herein we show that the N-terminal SH4 region of the Src family member p59(fyn) (Fyn) is both necessary and sufficient for targeting of Fyn and heterologous proteins to the plasma membrane and detergent-insoluble subdomains. Attachment of the first 16 amino acids of Fyn to a normally cytosolic protein, beta-galactosidase, resulted in distinct plasma membrane localization of the chimeric protein. Mutation of the palmitoylation site (cysteine-3) within Fyn16-beta-galactosidase or wildtype Fyn abrogated plasma membrane localization, resulting in redistribution of the mutant proteins into intracellular membranes. Substitution of the SH4 motif within Fyn with heterologous sequences from other palmitoylated proteins (G alpha o and GAP43) revealed that the presence of palmitate is sufficient to direct plasma membrane localization independent of surroundingamino acid sequences and myristate. Palmitoylated Fyn chimeras were also enriched in the Triton X-100-resistant matrix, whereas nonpalmitoylated forms of these proteins were detected in the detergent-soluble fraction. The palmitate moiety on Fyn exhibited a half-life of 1.5-2 h. In contrast, the half-life of the polypeptide backbone was 8 h, indicating that palmitoylation is a reversible modification. These studies establish that the palmitoylated SH4 sequence of Fyn can be used to specifically target proteins to the plasma membrane in a reversible manner.

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Documento generato il 29/09/20 alle ore 23:57:48