Publication Date:
1999-07-03
Description:
Regulation of N-methyl-D-aspartate (NMDA) receptor activity by kinases and phosphatases contributes to the modulation of synaptic transmission. Targeting of these enzymes near the substrate is proposed to enhance phosphorylation-dependent modulation. Yotiao, an NMDA receptor-associated protein, bound the type I protein phosphatase (PP1) and the adenosine 3',5'-monophosphate (cAMP)-dependent protein kinase (PKA) holoenzyme. Anchored PP1 was active, limiting channel activity, whereas PKA activation overcame constitutive PP1 activity and conferred rapid enhancement of NMDA receptor currents. Hence, yotiao is a scaffold protein that physically attaches PP1 and PKA to NMDA receptors to regulate channel activity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Westphal, R S -- Tavalin, S J -- Lin, J W -- Alto, N M -- Fraser, I D -- Langeberg, L K -- Sheng, M -- Scott, J D -- F32 NS010202/NS/NINDS NIH HHS/ -- GM 48231/GM/NIGMS NIH HHS/ -- NS10202/NS/NINDS NIH HHS/ -- NS10543/NS/NINDS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1999 Jul 2;285(5424):93-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Vollum Institute, Oregon Health Sciences University, 3181 S.W. Sam Jackson Road, Portland, OR 97201, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10390370" target="_blank"〉PubMed〈/a〉
Keywords:
A Kinase Anchor Proteins
;
*Adaptor Proteins, Signal Transducing
;
Amino Acid Sequence
;
Animals
;
Binding Sites
;
Carrier Proteins/*metabolism
;
Cell Line
;
Cyclic AMP/analogs & derivatives/pharmacology
;
Cyclic AMP-Dependent Protein Kinases/*metabolism
;
Cytoskeletal Proteins/*metabolism
;
Enzyme Inhibitors/pharmacology
;
Holoenzymes/metabolism
;
Humans
;
Molecular Sequence Data
;
Okadaic Acid/pharmacology
;
Patch-Clamp Techniques
;
Peptide Fragments/pharmacology
;
Phosphoprotein Phosphatases/*metabolism
;
Phosphorylation
;
Rats
;
Receptors, N-Methyl-D-Aspartate/*metabolism
;
Recombinant Fusion Proteins/metabolism
;
Signal Transduction
;
Thionucleotides/pharmacology
;
Transfection
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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