The Src homology 3 binding domain is required for lysophosphatidic acid 3 receptor-mediated cellular viability in melanoma cells

Highlights • Herein we elucidate the mechanism explaining the LPA3 receptor's ability to increase viability among melanoma cells. • The Src homology 3 ligand binding motif, (216)-KTNVLSP-(222), within the third intracellular loop of LPA3 mediates viability. • We perform a series of site-directe...

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Bibliographic Details
Published in:	Cancer letters Vol. 356; no. 2; pp. 589 - 596
Main Authors:	Jia, Wei, Tran, Sterling K, Ruddick, Caitlin A, Murph, Mandi M
Format:	Journal Article
Language:	English
Published:	Ireland Elsevier Ireland Ltd 28-01-2015 Elsevier Limited
Subjects:	Adapter proteins Amino Acid Sequence Apoptosis Binding sites Blotting, Western Calcium - metabolism Cancer Cancer therapies Cell Proliferation Chemotherapy Epigenetics Fluorescent Antibody Technique Gene expression Hematology, Oncology and Palliative Medicine Humans Kinases Ligands LPA3 Lysophosphatidic acid Melanoma Melanoma - genetics Melanoma - metabolism Melanoma - pathology Molecular Sequence Data Mutagenesis, Site-Directed Mutation - genetics Receptors, Lysophosphatidic Acid - genetics Receptors, Lysophosphatidic Acid - metabolism Sequence Homology, Amino Acid SH3 domain Signal transduction src Homology Domains Studies Tumor Cells, Cultured Wound healing SH3 domain Lysophosphatidic acid LPA 3 LPA3 LPA
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Summary:	Highlights • Herein we elucidate the mechanism explaining the LPA3 receptor's ability to increase viability among melanoma cells. • The Src homology 3 ligand binding motif, (216)-KTNVLSP-(222), within the third intracellular loop of LPA3 mediates viability. • We perform a series of site-directed mutagenesis assays to uncover this role.
ISSN:	0304-3835 1872-7980
DOI:	10.1016/j.canlet.2014.10.001