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Immunolocalization of the cellular src protein in interphase and mitotic NIH c-src overexpresser cells.
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MedLine Citation:
PMID:  1702788     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The mouse mAb, mAb 327, that recognizes specifically both pp60v-src and pp60c-src in a wide variety of cells, has been used to determine precisely the various locations of pp60c-src in NIH c-src overexpresser cells, using the technique of immunofluorescence microscopy. In interphase cells, the protein exhibits two main distributions: one that appears uniform and in association with the cell surface and the other that is patchy and juxtanuclear and coincides with the centrosomes. The juxtanuclear aggregation of pp60c-src-containing patches depends on microtubules and does not seem to occur within the Golgi apparatus and the rough ER. At the G2-to-M-phase transition, a drastic change in the localization patterns of pp60c-src takes place. We also report experiments in which the NIH c-src overexpresser cells were exposed to Con A for various times to induce a redistribution of the cell surface Con A receptors. We show that, at each stage of the Con A-mediated endocytotic process, the Con A-receptor complexes redistribute into structures to which pp60c-src appears also to be associated: at first, into patches that form at the cell surface level and then, into a cap that stands at the cell center in a juxtanuclear position and that coincides with the Golgi apparatus. During this capping process, pp60c-src-containing vesicles continue to accumulate in a centriolar spot, as in interphase, Con A-untreated cells, from which Con A is excluded. The significance of the intracellular locations of pp60c-src to the possible functions of the protein is discussed. Also, the distribution patterns of the cellular protein in the NIH c-src overexpresser cells are compared with those of pp60v-src in RSV-transformed cells. The differences observed are discussed in relation with the differences in transforming capacities of the two proteins. Finally, the possible physiological significance of the association between pp60c-src and the structures generated after the binding of Con A to its surface receptors is addressed.
Authors:
T David-Pfeuty; Y Nouvian-Dooghe
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  The Journal of cell biology     Volume:  111     ISSN:  0021-9525     ISO Abbreviation:  J. Cell Biol.     Publication Date:  1990 Dec 
Date Detail:
Created Date:  1991-02-21     Completed Date:  1991-02-21     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  0375356     Medline TA:  J Cell Biol     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  3097-116     Citation Subset:  IM    
Affiliation:
Institut Curie-Biologie, Centre Universitaire, Orsay, France.
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MeSH Terms
Descriptor/Qualifier:
Animals
Cell Adhesion / physiology
Cell Compartmentation
Cell Line
Concanavalin A / metabolism
Endocytosis / physiology
Fluorescent Dyes
Immunohistochemistry
Interphase / physiology*
Mitosis / physiology*
Proto-Oncogene Proteins pp60(c-src) / analysis*,  physiology
Recombinant Proteins / analysis
Transfection
Chemical
Reg. No./Substance:
0/Fluorescent Dyes; 0/Recombinant Proteins; 11028-71-0/Concanavalin A; EC 2.7.10.2/Proto-Oncogene Proteins pp60(c-src)
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

Full Text
Journal Information
Journal ID (nlm-ta): J Cell Biol
ISSN: 0021-9525
ISSN: 1540-8140
Publisher: The Rockefeller University Press
Article Information
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Print publication date: Day: 1 Month: 12 Year: 1990
Volume: 111 Issue: 6
First Page: 3097 Last Page: 3116
ID: 2116410
Publisher Id: 91100422
PubMed Id: 1702788

Immunolocalization of the cellular src protein in interphase and mitotic NIH c-src overexpresser cells


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