کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
2048528 1074083 2011 9 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Chelerythrine perturbs lamellar actomyosin filaments by selective inhibition of myotonic dystrophy kinase-related Cdc42-binding kinase
موضوعات مرتبط
علوم زیستی و بیوفناوری علوم کشاورزی و بیولوژیک دانش گیاه شناسی
پیش نمایش صفحه اول مقاله
Chelerythrine perturbs lamellar actomyosin filaments by selective inhibition of myotonic dystrophy kinase-related Cdc42-binding kinase
چکیده انگلیسی

Cell movement requires forces generated by non-muscle myosin II (NM II) for coordinated protrusion and retraction. The Cdc42/Rac effector MRCK regulates a specific actomyosin network in the lamella essential for cell protrusion and migration. Together with the Rho effector ROK required for cell rear retraction, they cooperatively regulate cell motility and tumour cell invasion. Despite the increasing importance of ROK inhibitors for both experimental and clinical purposes, there is a lack of specific inhibitors for other related kinases such as MRCK. Here, we report the identification of chelerythrine chloride as a specific MRCK inhibitor. Its ability to block cellular activity of MRCK resulted in the specific loss of NM II-associated MLC phosphorylation in the lamella, and the consequential suppression of cell migration.Structured summary of protein interactionsDMPKphosphorylatesMYPT by protein kinase assay(View interaction)PAK alphaphosphorylatesMLC by protein kinase assay(View interaction)MRCK alphaphosphorylatesMLC by protein kinase assay(View interaction)CRIKphosphorylatesMLC by protein kinase assay(View interaction)MRCKbeta phosphorylatesMLC by protein kinase assay(View interaction)ROK alphaphosphorylatesMLC by protein kinase assay (View Interaction 1, 2)MRCK betaphosphorylatesMYPT by protein kinase assay(View interaction)MRCK alphaphosphorylatesMYPT by protein kinase assay(View interaction)ROK alphaphosphorylatesMYPT by protein kinase assay(View interaction)MLCKphosphorylatesMLC by protein kinase assay(View interaction)

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: FEBS Letters - Volume 585, Issue 9, 6 May 2011, Pages 1260–1268
نویسندگان
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