Association of p60c-src with endosomal membranes in mammalian fibroblasts. Academic Article uri icon

Overview

abstract

  • We have examined the subcellular localization of p60c-src in mammalian fibroblasts. Analysis of indirect immunofluorescence by three-dimensional optical sectioning microscopy revealed a granular cytoplasmic staining that co-localized with the microtubule organizing center. Immunofluorescence experiments with antibodies against a number of membrane markers demonstrated a striking co-localization between p60c-src and the cation-dependent mannose-6-phosphate receptor (CI-MPR), a marker that identifies endosomes. Both p60c-src and the CI-MPR were found to cluster at the spindle poles throughout mitosis. In addition, treatment of interphase and mitotic cells with brefeldin A resulted in a clustering of p60c-src and CI-MPR at a peri-centriolar position. Biochemical fractionation of cellular membranes showed that a major proportion of p60c-src co-enriched with endocytic membranes. Treatment of membranes containing HRP to alter their apparent density also altered the density of p60c-src-containing membranes. Similar density shift experiments with total cellular membranes revealed that the majority of membrane-associated p60c-src in the cell is associated with endosomes, while very little is associated with plasma membranes. These results support a role for p60c-src in the regulation of endosomal membranes and protein trafficking.

publication date

  • July 1, 1992

Research

keywords

  • Cytoplasmic Granules
  • Endocytosis
  • Intracellular Membranes
  • Microtubules
  • Proto-Oncogene Proteins pp60(c-src)

Identity

PubMed Central ID

  • PMC2290043

Scopus Document Identifier

  • 0026611047

Digital Object Identifier (DOI)

  • 10.1083/jcb.118.2.321

PubMed ID

  • 1378446

Additional Document Info

volume

  • 118

issue

  • 2