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Transmodulation between phospholipase D and c-Src enhances cell proliferation.

التفاصيل البيبلوغرافية
العنوان: Transmodulation between phospholipase D and c-Src enhances cell proliferation.
المؤلفون: Ahn, BH, Kim, SY, Kim, EH, Choi, KS, Kwon, TK, Lee, YH, Chang, JS, Kim, MS, Jo, YH, Min, DS
المساهمون: 102263, 최, 경숙
سنة النشر: 2003
مصطلحات موضوعية: Animals, Carcinoma, Squamous Cell, Catalytic Domain, Cell Division, Cells, Cultured, Cytoskeletal Proteins, Enzyme Activation, Epidermal Growth Factor, Female, Humans, Mice, Inbred BALB C, Mitogen-Activated Protein Kinases, Mutation, Paxillin, Phospholipase D, Phosphoproteins, Phosphorylation, Protein Structure, Tertiary, Protein-Tyrosine Kinases, Rats, Signal Transduction, Tyrosine
الوصف: Phospholipase D (PLD) has been implicated in the signal transduction pathways initiated by several mitogenic protein tyrosine kinases. We demonstrate for the first time that most notably PLD2 and to a lesser extent the PLD1 isoform are tyrosine phosphorylated by c-Src tyrosine kinase via direct association. Moreover, epidermal growth factor induced tyrosine phosphorylation of PLD2 and its interaction with c-Src in A431 cells. Interaction between these proteins is via the pleckstrin homology domain of PLD2 and the catalytic domain of c-Src. Coexpression of PLD1 or PLD2 with c-Src synergistically enhances cellular proliferation compared with expression of either molecule. While PLD activity as a lipid-hydrolyzing enzyme is not affected by c-Src, wild-type PLDs but not catalytically inactive PLD mutants significantly increase c-Src kinase activity, up-regulating c-Src-mediated paxillin phosphorylation and extracellular signal-regulated kinase activity. These results demonstrate the critical role of PLD catalytic activity in the stimulation of Src signaling. In conclusion, we provide the first evidence that c-Src acts as a kinase of PLD and PLD acts as an activator of c-Src. This transmodulation between c-Src and PLD may contribute to the promotion of cellular proliferation via amplification of mitogenic signaling pathways.
نوع الوثيقة: article in journal/newspaper
وصف الملف: text/plain
اللغة: English
تدمد: 0270-7306
1098-5549
Relation: J002707306; http://repository.ajou.ac.kr/handle/201003/3659; https://www.ncbi.nlm.nih.gov/pmc/articles/PMC153190/; PMID-12697812; Molecular and cellular biology, 23(9). : 3103-3115, 2003
الاتاحة: http://repository.ajou.ac.kr/handle/201003/3659
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC153190/
رقم الانضمام: edsbas.10B4A16
قاعدة البيانات: BASE
الوصف
تدمد:02707306
10985549