Linked Life Data

21145357

Source:http://linkedlifedata.com/resource/pubmed/id/21145357

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2011-1-24
pubmed:abstractText
Internalization of H-Ras from the cell surface onto endomembranes through vesicular endocytic pathways may play a significant role(s) in regulating the outcome of Ras signaling. However, the identity of Ras-associated subcellular vesicles and the means by which Ras localize to these internal sites remain elusive. In this study, we show that H-Ras is absent from endosomes initially derived from a clathrin-dependent endocytic pathway. Instead, both oncogenic H-Ras-61L and wild type H-Ras (basal or EGF-stimulated) bind Arf6-associated clathrin-independent endosomes and vesicles of the endosomal-recycling center (ERC). K-Ras4B-12V can also be internalized via Arf6 endosomes, and the C-terminal tails of both H-Ras and K-Ras4B are sufficient to mediate localization of GFP chimeras to Arf6-associated vesicles. Interestingly, little Raf-1 was found on these Arf6-associated endosomes even when active H-Ras was present. Instead, endogenous Raf-1 distributed primarily on EEA1-containing vesicles, suggesting that this H-Ras effector, although accessible for H-Ras interaction on the plasma membrane, appears to separate from its regulator during early stages of endocytosis. The discrete and dynamic distribution of Ras pathway components with spatio-temporal complexity may contribute to the specificity of Ras:effector interaction.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0006-3002
pubmed:author
pubmed:copyrightInfo
2010 Elsevier B.V. All rights reserved.
pubmed:issnType
Print
pubmed:volume
1813
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
298-307
pubmed:meshHeading
pubmed-meshheading:21145357-ADP-Ribosylation Factors, pubmed-meshheading:21145357-Animals, pubmed-meshheading:21145357-Blotting, Western, pubmed-meshheading:21145357-Cell Membrane, pubmed-meshheading:21145357-Clathrin, pubmed-meshheading:21145357-Endocytosis, pubmed-meshheading:21145357-Endosomes, pubmed-meshheading:21145357-Fluorescent Antibody Technique, pubmed-meshheading:21145357-Green Fluorescent Proteins, pubmed-meshheading:21145357-Humans, pubmed-meshheading:21145357-Mice, pubmed-meshheading:21145357-NIH 3T3 Cells, pubmed-meshheading:21145357-Proto-Oncogene Proteins c-raf, pubmed-meshheading:21145357-Proto-Oncogene Proteins p21(ras), pubmed-meshheading:21145357-Signal Transduction, pubmed-meshheading:21145357-Transport Vesicles, pubmed-meshheading:21145357-Vesicular Transport Proteins
pubmed:year
2011
pubmed:articleTitle
H-ras resides on clathrin-independent ARF6 vesicles that harbor little RAF-1, but not on clathrin-dependent endosomes.
pubmed:affiliation
Department of Biochemistry, Biophysics and Molecular Biology, Iowa State University, Ames, IA 50011-3260, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S.