Click
here to close Hello! We notice that
you are using Internet Explorer, which is not supported by Echinobase
and may cause the site to display incorrectly. We suggest using a
current version of Chrome,
FireFox,
or Safari.
Mol Cell Biochem
1995 Nov 08;1521:63-70. doi: 10.1007/bf01076464.
Show Gene links
Show Anatomy links
Phosphorylation of the carboxyl terminal region of dystrophin by mitogen-activated protein (MAP) kinase.
Shemanko CS
,
Sanghera JS
,
Milner RE
,
Pelech S
,
Michalak M
.
???displayArticle.abstract???
Dystrophin is the 427-kDa protein product of the Duchenne muscular dystrophy gene (DMD). The function of this protein remains to be elucidated. We have recently reported that dystrophin is phosphorylated, in vivo, in rat skeletal muscle primary cell culture (RE Milner, JL Busaan, CFB Holmes, JH Wang, M Michalak (1993) J Biol Chem 268:21901-21905). This observation suggests that protein phosphorylation may have some role in modulating the function of dystrophin or its interaction with membrane associate dystroglycan. We report here that the carboxyl-terminal of dystrophin is phosphorylated by the MAP kinase p44mpk (mitogen-activated protein kinase), from the sea star oocytes and by soluble extracts of rabbit skeletal muscle. Importantly we showed that native dystrophin in isolated sarcolemmal vesicles is phosphorylated by sea star p44mpk Partial purification and immunological analysis show that a mammalian kinase related to p44mpk is present in the skeletal muscle extracts and that it contributes to phosphorylation of the carboxyl-terminal of dystrophin. This kinase phosphorylates dystrophin on a threonine residue(s). We conclude that phosphorylation of dystrophin may play an important role in the function of this cytoskeletal protein.
Ahmad,
Purification and characterization of a rabbit liver calmodulin-dependent protein kinase able to phosphorylate glycogen synthase.
1982, Pubmed
Ahmad,
Purification and characterization of a rabbit liver calmodulin-dependent protein kinase able to phosphorylate glycogen synthase.
1982,
Pubmed
Ahn,
The structural and functional diversity of dystrophin.
1993,
Pubmed
Bar,
A novel product of the Duchenne muscular dystrophy gene which greatly differs from the known isoforms in its structure and tissue distribution.
1990,
Pubmed
Bennett,
Spectrin-based membrane skeleton: a multipotential adaptor between plasma membrane and cytoplasm.
1990,
Pubmed
Boulton,
ERKs: a family of protein-serine/threonine kinases that are activated and tyrosine phosphorylated in response to insulin and NGF.
1991,
Pubmed
Bowe,
Identification and purification of an agrin receptor from Torpedo postsynaptic membranes: a heteromeric complex related to the dystroglycans.
1994,
Pubmed
Byers,
An alternative dystrophin transcript specific to peripheral nerve.
1993,
Pubmed
Campanelli,
A role for dystrophin-associated glycoproteins and utrophin in agrin-induced AChR clustering.
1994,
Pubmed
Charest,
Molecular cloning, expression, and characterization of the human mitogen-activated protein kinase p44erk1.
1993,
Pubmed
Childs,
Phosphorylation of smooth muscle caldesmon by mitogen-activated protein (MAP) kinase and expression of MAP kinase in differentiated smooth muscle cells.
1992,
Pubmed
,
Echinobase
Clark-Lewis,
Definition of a consensus sequence for peptide substrate recognition by p44mpk, the meiosis-activated myelin basic protein kinase.
1991,
Pubmed
,
Echinobase
Gee,
Dystroglycan-alpha, a dystrophin-associated glycoprotein, is a functional agrin receptor.
1994,
Pubmed
Gotoh,
In vitro effects on microtubule dynamics of purified Xenopus M phase-activated MAP kinase.
1991,
Pubmed
Jones,
Rapid preparation of canine cardiac sarcolemmal vesicles by sucrose flotation.
1988,
Pubmed
Laemmli,
Cleavage of structural proteins during the assembly of the head of bacteriophage T4.
1970,
Pubmed
LOWRY,
Protein measurement with the Folin phenol reagent.
1951,
Pubmed
Luise,
Dystrophin is phosphorylated by endogenous protein kinases.
1993,
Pubmed
Madhavan,
Calmodulin-activated phosphorylation of dystrophin.
1994,
Pubmed
Matsumura,
Dystrophin-glycoprotein complex: its role in the molecular pathogenesis of muscular dystrophies.
1994,
Pubmed
Meyerson,
A family of human cdc2-related protein kinases.
1992,
Pubmed
Milner,
Isolation and characterization of different C-terminal fragments of dystrophin expressed in Escherichia coli.
1992,
Pubmed
Milner,
Phosphorylation of dystrophin. The carboxyl-terminal region of dystrophin is a substrate for in vitro phosphorylation by p34cdc2 protein kinase.
1993,
Pubmed
Moreno,
Substrates for p34cdc2: in vivo veritas?
1990,
Pubmed
Nishida,
The MAP kinase cascade is essential for diverse signal transduction pathways.
1993,
Pubmed
Pelech,
MAP kinases: charting the regulatory pathways.
1992,
Pubmed
Pelech,
Mitogen-activated protein kinases: versatile transducers for cell signaling.
1992,
Pubmed
Sanghera,
Immunological characterization of avian MAP kinases: evidence for nuclear localization.
1992,
Pubmed
,
Echinobase
Sanghera,
Identification of epidermal growth factor Thr-669 phosphorylation site peptide kinases as distinct MAP kinases and p34cdc2.
1992,
Pubmed
,
Echinobase
Stokoe,
MAPKAP kinase-2; a novel protein kinase activated by mitogen-activated protein kinase.
1992,
Pubmed
Suzuki,
Glycoprotein-binding site of dystrophin is confined to the cysteine-rich domain and the first half of the carboxy-terminal domain.
1992,
Pubmed
Tamemoto,
Biphasic activation of two mitogen-activated protein kinases during the cell cycle in mammalian cells.
1992,
Pubmed
Tinsley,
Primary structure of dystrophin-related protein.
1992,
Pubmed
Towbin,
Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications.
1979,
Pubmed
Wagner,
The 87K postsynaptic membrane protein from Torpedo is a protein-tyrosine kinase substrate homologous to dystrophin.
1993,
Pubmed
