Prolactin-induced PAK1 tyrosyl phosphorylation promotes FAK dephosphorylation, breast cancer cell motility, invasion and metastasis

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• 作者：Alan Hammer ; Maria Diakonova
• 关键词：PAK1 ; FAK ; Prolactin ; Tyrosyl phosphorylation ; Breast cancer cells
• 刊名：BMC Cell Biology
• 出版年：2016
• 出版时间：December 2016
• 年：2016
• 卷：17
• 期：1
• 全文大小：1703KB
• 刊物主题：Cell Biology; Biological Microscopy; Life Sciences, general;
• 出版者：BioMed Central
• ISSN：1471-2121
• 卷排序：17

文摘

BackgroundThe serine/threonine kinase PAK1 is an important regulator of cell motility. Both PAK1 and the hormone/cytokine prolactin (PRL) have been implicated in breast cancer cell motility, however, the exact mechanisms guiding PRL/PAK1 signaling in breast cancer cells have not been fully elucidated. Our lab has previously demonstrated that PRL-activated tyrosine kinase JAK2 phosphorylates PAK1 on tyrosines 153, 201, and 285, and that tyrosyl phosphorylated PAK1 (pTyr-PAK1) augments migration and invasion of breast cancer cells.