PMID- 10525145
OWN - NLM
STAT- MEDLINE
DCOM- 19991116
LR  - 20190610
IS  - 0006-3002 (Print)
IS  - 0006-3002 (Linking)
VI  - 1434
IP  - 2
DP  - 1999 Oct 12
TI  - Phosphorylation of dystrophin and alpha-syntrophin by Ca(2+)-calmodulin dependent
      protein kinase II.
PG  - 260-74
AB  - A Ca(2+)-calmodulin dependent protein kinase activity (DGC-PK) was previously
      shown to associate with skeletal muscle dystrophin glycoprotein complex (DGC)
      preparations, and phosphorylate dystrophin and a protein with the same
      electrophoretic mobility as alpha-syntrophin (R. Madhavan, H.W. Jarrett,
      Biochemistry 33 (1994) 5797-5804). Here, we show that DGC-PK and
      Ca(2+)-calmodulin dependent protein kinase II (CaM kinase II) phosphorylate a
      common site (RSDS(3616)) within the dystrophin C terminal domain that fits the
      consensus CaM kinase II phosphorylation motif (R/KXXS/T). Furthermore, both
      kinase activities phosphorylate exactly the same three fusion proteins
      (dystrophin fusions DysS7 and DysS9, and the syntrophin fusion) out of a panel of
      eight fusion proteins (representing nearly 100% of syntrophin and 80% of
      dystrophin protein sequences), demonstrating that DGC-PK and CaM kinase II have
      the same substrate specificity. Complementing these results, anti-CaM kinase II
      antibodies specifically stained purified DGC immobilized on nitrocellulose
      membranes. Renaturation of electrophoretically resolved DGC proteins revealed a
      single protein kinase band (M(r) approximately 60,000) that, like CaM kinase II, 
      underwent Ca(2+)-calmodulin dependent autophosphorylation. Based on these
      observations, we conclude DGC-PK represents a
      dystrophin-/syntrophin-phosphorylating skeletal muscle isoform of CaM kinase II. 
      We also show that phosphorylation of the dystrophin C terminal domain sequences
      inhibits their syntrophin binding in vitro, suggesting a regulatory role for
      phosphorylation.
FAU - Madhavan, R
AU  - Madhavan R
AD  - Department of Biochemistry, University of Tennessee-Memphis, 858 Madison Ave.,
      Memphis, TN 38163, USA.
FAU - Jarrett, H W
AU  - Jarrett HW
LA  - eng
GR  - NS33145/NS/NINDS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - Netherlands
TA  - Biochim Biophys Acta
JT  - Biochimica et biophysica acta
JID - 0217513
RN  - 0 (Antibodies)
RN  - 0 (Calcium-Binding Proteins)
RN  - 0 (Cytoskeletal Proteins)
RN  - 0 (Dystrophin)
RN  - 0 (Isoenzymes)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Membrane Proteins)
RN  - 0 (Muscle Proteins)
RN  - 0 (Sarcoglycans)
RN  - 0 (syntrophin alpha1)
RN  - 8L70Q75FXE (Adenosine Triphosphate)
RN  - EC 2.7.11.17 (Calcium-Calmodulin-Dependent Protein Kinase Type 2)
RN  - EC 2.7.11.17 (Calcium-Calmodulin-Dependent Protein Kinases)
RN  - EC 3.4.21.4 (Trypsin)
SB  - IM
MH  - Adenosine Triphosphate/chemistry
MH  - Animals
MH  - Antibodies/immunology
MH  - Blotting, Western
MH  - Calcium-Binding Proteins
MH  - Calcium-Calmodulin-Dependent Protein Kinase Type 2
MH  - Calcium-Calmodulin-Dependent Protein Kinases/*chemistry/immunology/isolation &
      purification
MH  - Cytoskeletal Proteins/chemistry
MH  - Dystrophin/*chemistry
MH  - Isoenzymes/chemistry/immunology
MH  - Membrane Glycoproteins/chemistry
MH  - Membrane Proteins/*chemistry
MH  - Muscle Proteins/*chemistry
MH  - Muscle, Skeletal/enzymology
MH  - Muscular Dystrophy, Duchenne/enzymology
MH  - Phosphorylation
MH  - Rabbits
MH  - Sarcoglycans
MH  - Signal Transduction
MH  - Trypsin
EDAT- 1999/10/19 00:00
MHDA- 1999/10/19 00:01
CRDT- 1999/10/19 00:00
PHST- 1999/10/19 00:00 [pubmed]
PHST- 1999/10/19 00:01 [medline]
PHST- 1999/10/19 00:00 [entrez]
AID - S0167-4838(99)00193-4 [pii]
AID - 10.1016/s0167-4838(99)00193-4 [doi]
PST - ppublish
SO  - Biochim Biophys Acta. 1999 Oct 12;1434(2):260-74. doi:
      10.1016/s0167-4838(99)00193-4.