DOI: 10.1083/jcb.137.5.1029. Intrinsic Signals in the Unique Domain Target p56<i>lck</i>to the Plasma Membrane Independently of CD4

Intrinsic Signals in the Unique Domain Target p56lckto the Plasma Membrane Independently of CD4

10.1083/jcb.137.5.1029

Crossref journal-article

Rockefeller University Press

The Journal of Cell Biology (291)

Abstract

In T lymphocytes, the Src-family protein tyrosine kinase p56lck (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 exocytic transport vesicles. A mutant Lck molecule in which the palmitoylation site at cysteine 5 was changed to lysine (LC2) localized to the plasma membrane and the Golgi region in NIH3T3 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.

Bibliography

Bijlmakers, M.-J. J. E., Isobe-Nakamura, M., Ruddock, L. J., & Marsh, M. (1997). Intrinsic Signals in the Unique Domain Target p56lckto the Plasma Membrane Independently of CD4. The Journal of Cell Biology, 137(5), 1029â1040.

Authors 4

Marie-José J.E. Bijlmakers (first)
Misako Isobe-Nakamura (additional)
Lindsay J. Ruddock (additional)
Mark Marsh (additional)

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Dates

Type	When
Created	23 years, 1 month ago (July 26, 2002, 12:47 p.m.)
Deposited	2 years, 1 month ago (July 28, 2023, 6:44 p.m.)
Indexed	4 months, 4 weeks ago (April 1, 2025, 2:03 a.m.)
Issued	28 years, 2 months ago (June 2, 1997)
Published	28 years, 2 months ago (June 2, 1997)
Published Online	28 years, 2 months ago (June 2, 1997)
Published Print	28 years, 2 months ago (June 2, 1997)

Funders 0

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BibTeX

@article{Bijlmakers_1997, title={Intrinsic Signals in the Unique Domain Target p56lckto the Plasma Membrane Independently of CD4}, volume={137}, ISSN={1540-8140}, url={http://dx.doi.org/10.1083/jcb.137.5.1029}, DOI={10.1083/jcb.137.5.1029}, number={5}, journal={The Journal of Cell Biology}, publisher={Rockefeller University Press}, author={Bijlmakers, Marie-José J.E. and Isobe-Nakamura, Misako and Ruddock, Lindsay J. and Marsh, Mark}, year={1997}, month=jun, pages={1029–1040} }

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  "abstract": "<jats:p>In T lymphocytes, the Src-family protein tyrosine kinase p56lck (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\u2013specific 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 exocytic transport vesicles.</jats:p>\n               <jats:p>A mutant Lck molecule in which the palmitoylation site at cysteine 5 was changed to lysine (LC2) localized to the plasma membrane and the Golgi region in NIH3T3 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.</jats:p>",
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