Abstract
Overexpression of the c-src proto-oncogene product with its increased kinase activity is observed in numerous cancer types. Oncogenic transformation is often associated with aberrant lysosome distribution. Here, we show that v-Src and c-Src, nonpalmitoylated Src kinases, largely localize to lysosomes and induce perinuclear accumulation of lysosomes through Rab7 in a manner dependent on the SH2 domain but dispensable for the kinase activity. Unlike v-Src and c-Src, the palmitoylated Src kinases c-Yes, Fyn and Lyn localize minimally to lysosomes and marginally affect lysosome distribution. These results suggest that elevated expression of nonpalmitoylated Src plays a critical role in lysosome distribution.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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COS Cells
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Chlorocebus aethiops
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HeLa Cells
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Humans
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Lipoylation
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Lysosomes / physiology*
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Oncogene Protein pp60(v-src) / metabolism*
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Proto-Oncogene Mas
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Proto-Oncogene Proteins c-fyn / metabolism
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Proto-Oncogene Proteins c-yes / metabolism
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Proto-Oncogene Proteins pp60(c-src) / metabolism*
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rab GTP-Binding Proteins / metabolism*
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rab7 GTP-Binding Proteins
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src-Family Kinases / metabolism
Substances
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MAS1 protein, human
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Proto-Oncogene Mas
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rab7 GTP-Binding Proteins
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rab7 GTP-binding proteins, human
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Oncogene Protein pp60(v-src)
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Proto-Oncogene Proteins c-fyn
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Proto-Oncogene Proteins c-yes
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Proto-Oncogene Proteins pp60(c-src)
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lyn protein-tyrosine kinase
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src-Family Kinases
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rab GTP-Binding Proteins