mik1+ encodes a tyrosine kinase that phosphorylates p34cdc2 on tyrosine 15.
نویسندگان
چکیده
منابع مشابه
Cloning and biochemical characterization of a plant protein kinase that phosphorylates serine, threonine, and tyrosine.
Phosphorylation of proteins on serine, threonine, or tyrosine residues represents an important biochemical mechanism to regulate the activity of enzymes and is used in many cellular processes. In animals, protein serine/threonine and protein tyrosine kinases are known to perform essential roles in many pathways that transmit external stimuli from the cell surface to the cell inferior and the nu...
متن کاملFMS-like Tyrosine Kinase-3 Mutation in a Child with Standard-risk ALL and Normal Karyotype
FMS-like tyrosine kinase-3 is a receptor tyrosine kinase expressed by immature hematopoietic cells and is important for the normal development of stem cells and the immune system. Mutations of FMS-like tyrosine kinase-3 have been detected in about 30% of patients with acute myelogenous leukemia and a small number of patients with acute lymphoblastic leukemia. The FMS-like tyrosine kinase-3 muta...
متن کاملp34cdc2 is physically associated with and phosphorylated by a cdc2-specific tyrosine kinase.
The mammalian homologue of the yeast cdc2 gene encodes a 34-kilodalton serine/threonine kinase that is a subunit of M phase-promoting factor. Recent studies have shown that p34cdc2 is also a major tyrosine-phosphorylated protein in HeLa cells and that its phosphotyrosine content is cell cycle regulated and related to its kinase activity. Here, we show that cdc2 is physically associated with and...
متن کاملAbl Tyrosine Kinase Phosphorylates Nonmuscle Myosin Light Chain Kinase to Regulate Endothelial Barrier Function
Nonmuscle myosin light chain kinase (nmMLCK), a multi-functional cytoskeletal protein critical to vascular homeostasis, is highly regulated by tyrosine phosphorylation. We identified multiple novel c-Abl-mediated nmMLCK phosphorylation sites by mass spectroscopy analysis (including Y231, Y464, Y556, Y846) and examined their influence on nmMLCK function and human lung endothelial cell (EC) barri...
متن کاملSrc Tyrosine Kinase Phosphorylates Ve-cadherin in Response to Vegf : Identification of the Tyrosine 685 as the Unique Target Site
INTRODUCTION. We recently demonstrated that Vascular Endothelial (VE)-cadherin was phosphorylated in vivo in angiogenic conditions (1) and in inflammation (2). Furthermore, we found a permanent association of VEcadherin with Src kinase (1). Vascular Endothelial Growth Factor (VEGF), a key angiogenic and vascular permeability factor is involved in a large number of disease, is known to induce VE...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1994
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)43846-x