Evidence map›Paper›PMID 9166404›Full record

ArticleThe Journal of cell biology1997

Intrinsic signals in the unique domain target p56(lck) to the plasma membrane independently of CD4.

M J Bijlmakers, M Isobe-Nakamura, L J Ruddock, M Marsh

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
3.0field-weighted citation impact, top 8% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

34 citing papers in PubMed, 87 citations in OpenAlex.

  1. Review
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  6. T cell receptor (TCR) signaling in health and disease.Signal transduction and targeted therapy · 2021
    Review
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  20. The Src kinase Lck facilitates assembly of HIV-1 at the plasma membrane.Journal of immunology (Baltimore, Md. : 1950) · 2008
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

M J BijlmakersMedical Research Council Laboratory for Molecular Cell Biology and Department of Biochemistry, University College London, London WC1E 6BT, United Kingdom.
M Isobe-Nakamura
L J Ruddock
M Marsh
University College London · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

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 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.

Indexed as

3T3 CellsAnimalsBiological TransportCD4 AntigensCD8 AntigensCell MembraneCysteineFluorescent Antibody Technique, IndirectGolgi ApparatusHeLa CellsHumansLymphocyte Specific Protein Tyrosine Kinase p56(lck)MiceMicroscopy, ElectronPalmitic AcidProtein Sorting SignalsCD4 AntigensCD8 AntigensCysteineLymphocyte Specific Protein Tyrosine Kinase p56(lck)Palmitic AcidProtein Sorting Signalssrc-Family Kinases

Identifiers

PMID9166404
PMCPMC2136224
OpenAlexW2020279663

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.