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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
8
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pubmed:dateCreated |
2010-7-12
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pubmed:abstractText |
Galectin-3 (Gal3) has important roles in tumor transformation and metastasis. This study shows that c-Abl and Abl-related gene (Arg) associate with and phosphorylate Gal3. The SH (Src homology)3 domains of c-Abl/Arg bind to a P(80)GPPSGP motif of Gal3, and Tyr79 and Tyr118 are the major tyrosine phosphorylation sites. A consequence of this interaction and phosphorylation is the significant impairment of chaperone-mediated autophagy of Gal3. Cells expressing Gal3 and treated with the c-Abl/Arg inhibitor STI571, Gal3-depleted cells, and Gal3-depleted cells expressing Gal3 phosphorylation mutants all display an increased sensitivity to apoptosis-inducing agents. In addition, tumor cells expressing the phosphorylation mutants show impaired tumorigenicity. These results partially explain the antiapoptotic effect of Abl and Arg. As tumors frequently overexpress Gal3, a c-Abl/Arg-specific inhibitor may potentially be applied along with other antitumor drugs to target the lysosomal degradation of Gal3 in tumor therapy.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
1476-5403
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pubmed:author |
pubmed-author:JiG FGF,
pubmed-author:JinYY,
pubmed-author:LULL,
pubmed-author:LiPP,
pubmed-author:LimPP,
pubmed-author:MOGG,
pubmed-author:OOIS KSK,
pubmed-author:QianXX,
pubmed-author:SoniNN,
pubmed-author:WangJJ,
pubmed-author:WangYY,
pubmed-author:YangYY,
pubmed-author:ZengJJ,
pubmed-author:ZhaoHH
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pubmed:issnType |
Electronic
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pubmed:volume |
17
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1277-87
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pubmed:meshHeading |
pubmed-meshheading:20150913-Animals,
pubmed-meshheading:20150913-Antineoplastic Agents,
pubmed-meshheading:20150913-Apoptosis,
pubmed-meshheading:20150913-Binding Sites,
pubmed-meshheading:20150913-Cell Line, Tumor,
pubmed-meshheading:20150913-Galectin 3,
pubmed-meshheading:20150913-Gene Knockdown Techniques,
pubmed-meshheading:20150913-Humans,
pubmed-meshheading:20150913-Lysosomes,
pubmed-meshheading:20150913-Mice,
pubmed-meshheading:20150913-Mice, Nude,
pubmed-meshheading:20150913-Phosphorylation,
pubmed-meshheading:20150913-Piperazines,
pubmed-meshheading:20150913-Protein Binding,
pubmed-meshheading:20150913-Protein-Tyrosine Kinases,
pubmed-meshheading:20150913-Proto-Oncogene Proteins c-abl,
pubmed-meshheading:20150913-Pyrimidines,
pubmed-meshheading:20150913-RNA Interference,
pubmed-meshheading:20150913-Xenograft Model Antitumor Assays,
pubmed-meshheading:20150913-src Homology Domains
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pubmed:year |
2010
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pubmed:articleTitle |
c-Abl and Arg tyrosine kinases regulate lysosomal degradation of the oncoprotein Galectin-3.
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pubmed:affiliation |
Beijing Institute of Biotechnology, Beijing, China.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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