Association of protein phosphatase 1γ1 with spinophilin suppresses phosphatase activity in a Parkinson disease model

Journal of Biological Chemistry

Volumn 283, Issue 21, 2008, Pages 14286-14294

  Brown, Abigail M ^a   Baucum, Anthony J ^a,b   Bass, Martha A ^a   Colbran, Roger J ^a,b,c  

^a VANDERBILT UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b VANDERBILT UNIVERSITY   (United States)

^c VANDERBILT UNIVERSITY MEDICAL CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CHEMICAL REACTIONS; DENDRIMERS; MODULATION; NIOBIUM; PHOSPHORYLATION; PLASTICITY; PROTEINS;

BINDING PROTEINS; DENDRITIC MORPHOLOGIES; HYPERPHOSPHORYLATION; IMMUNOPRECIPITATION; ISOFORM; ISOFORMS; LYSATES; MULTIPLE SUBSTRATES; PARKINSON DISEASES; PHOSPHATASE ACTIVITIES; PROTEIN KINASES; PROTEIN PHOSPHATASES; PROTEIN PHOSPHORYLATIONS; RAT STRIATUM; SELECTIVE INHIBITIONS; SERINE/THREONINE PHOSPHORYLATIONS; SYNAPTIC PLASTICITIES; SYNAPTIC PROTEINS;

BRAIN;

CALCIUM CALMODULIN DEPENDENT PROTEIN KINASE 2ALPHA; CALCIUM CALMODULIN DEPENDENT PROTEIN KINASE II; CARRIER PROTEINS AND BINDING PROTEINS; DOPAMINE; NEURABIN 1; PHOSPHOPROTEIN PHOSPHATASE; PHOSPHOPROTEIN PHOSPHATASE 2A; PROTEIN PHOSPHATAE 1GAMMA1; SPINOPHILIN; UNCLASSIFIED DRUG; ACTIN BINDING PROTEIN; ISOENZYME; NERVE PROTEIN; NEURABIN; PEPTIDE FRAGMENT; PHOSPHOPROTEIN PHOSPHATASE 1;

ANIMAL EXPERIMENT; ANIMAL MODEL; ARTICLE; AUTOPHOSPHORYLATION; CONTROLLED STUDY; CORPUS STRIATUM; ENZYME ACTIVITY; ENZYME INHIBITION; ENZYME SUBSTRATE; MALE; NONHUMAN; PARKINSON DISEASE; PRIORITY JOURNAL; PROTEIN DEPHOSPHORYLATION; PROTEIN DEPLETION; PROTEIN FUNCTION; RAT; ANIMAL; DISEASE MODEL; DRUG EFFECT; ENZYME ACTIVATION; ENZYME ACTIVE SITE; ENZYMOLOGY; METABOLISM; PHOSPHORYLATION; SPRAGUE DAWLEY RAT;

RATTUS;

ANIMALS; CATALYTIC DOMAIN; DISEASE MODELS, ANIMAL; DOPAMINE; ENZYME ACTIVATION; ISOENZYMES; MALE; MICROFILAMENT PROTEINS; NERVE TISSUE PROTEINS; PARKINSON DISEASE; PEPTIDE FRAGMENTS; PHOSPHORYLATION; PROTEIN PHOSPHATASE 1; RATS; RATS, SPRAGUE-DAWLEY;

EID: 47249154345     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M801377200     Document Type: Article

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