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Titolo:
INTRINSIC SIGNALS IN THE UNIQUE DOMAIN TARGET P56(LCK) TO THE PLASMA-MEMBRANE INDEPENDENTLY OF CD4
Autore:
BIJLMAKERS MJJE; ISOBENAKAMURA M; RUDDOCK LJ; MARSH M;
Indirizzi:
UNIV LONDON UNIV COLL,MRC,MOL CELL BIOL LAB,GOWER ST LONDON WC1E 6BT ENGLAND UNIV LONDON UNIV COLL,MRC,MOL CELL BIOL LAB LONDON WC1E 6BT ENGLAND UNIV LONDON UNIV COLL,DEPT BIOCHEM LONDON WC1E 6BT ENGLAND
Titolo Testata:
The Journal of cell biology
fascicolo: 5, volume: 137, anno: 1997,
pagine: 1029 - 1040
SICI:
0021-9525(1997)137:5<1029:ISITUD>2.0.ZU;2-Q
Fonte:
ISI
Lingua:
ENG
Soggetto:
PROTEIN-TYROSINE KINASE; GREEN-FLUORESCENT PROTEIN; AMINO-TERMINAL DOMAIN; CELL-LINE; ENDOPLASMIC-RETICULUM; CYTOPLASMIC DOMAINS; LYMPHOCYTES-T; P56LCK; ASSOCIATION; LCK;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
66
Recensione:
Indirizzi per estratti:
Citazione:
M.J.J.E. Bijlmakers et al., "INTRINSIC SIGNALS IN THE UNIQUE DOMAIN TARGET P56(LCK) TO THE PLASMA-MEMBRANE INDEPENDENTLY OF CD4", The Journal of cell biology, 137(5), 1997, pp. 1029-1040

Abstract

In T lymphocytes, the Src-family protein tyrosine kinase p56(lck) (Lck) is mostly associated with the cytoplasmic face of the plasma membrane. To determine how this distribution is achieved, we analyzed the location of Lck in lymphoid and in transfected nonlymphoid cells by immunofluorescence. We found that in T cells Lck was targeted correctly, independently of the cell surface proteins CD4 and CD8 with which it interacts. Similarly, in transfected NIH-3T3 fibroblasts, Lck was localized at the plasma membrane, indicating that T cell-specific proteins are not required for targeting. Some variation in subcellular distribution was observed when Lck was expressed in HeLa and MDCK cells. In these cells, Lck associated with both the plasma membrane and the Golgi apparatus, while subsequent expression of CD4 resulted in the loss of Golgi-associated staining. Together, these data indicate that Lck contains intrinsic signals for targeting to the plasma membrane. Furthermore, delivery to this site may be achieved via association with exocytictransport vesicles. A mutant Lck molecule in which the palmitoylationsite at cysteine 5 was changed to lysine (LC2) localized to the plasma membrane and the Golgi region in NIH-3T3 cells. However, the localization of a mutant in which the palmitoylation site at cysteine 3 was changed to serine (LC1) was indistinguishable from wild-type Lck. Chimeras composed of only the unique domain of Lck linked to either c-Src or the green fluorescent protein similarly localized to the plasma membrane of NIH-3T3 cells. Thus, the targeting of Lck appears to be determined primarily by its unique domain and may be influenced by the use of different palmitoylation sites.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 30/03/20 alle ore 18:38:45