| pubmed-article:2549856 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2549856 | lifeskim:mentions | umls-concept:C0031686 | lld:lifeskim |
| pubmed-article:2549856 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:2549856 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:2549856 | pubmed:dateCreated | 1989-10-11 | lld:pubmed |
| pubmed-article:2549856 | pubmed:abstractText | Four major serine/threonine-specific protein phosphatase catalytic subunits are present in the cytoplasm of animal cells. Three of these enzymes, PP-1, PP-2A, and PP-2B, are members of the same gene family, while PP-2C appears to be distinct. PP-1, PP-2A, and PP-2B are complexed to other subunits in vivo, whereas PP-2C has only been isolated as a monomeric protein. PP-1, PP-2A, and PP-2C have broad and overlapping specificities in vitro, and account for virtually all measurable activity in tissue extracts toward a variety of phosphoproteins that regulate metabolism, muscle contractility, and other processes. Their precise functions in vivo are unknown, although important clues to the physiological roles of PP-1 and PP-2A are provided by the effects of okadaic acid and by the subcellular localization of PP-1. The active forms of PP-1 are largely particulate, and their association with subcellular structures is mediated by "targetting subunits" that direct PP-1 to particular locations, enhance its activity toward certain substrates, and confer important regulatory properties upon it. This concept is best established for the glycogen-bound enzymes in skeletal muscle and liver (PP-1G) and the myofibrillar form (PP-1M) in skeletal muscle. The activities of PP-1 and PP-2B are controlled by the second messengers cyclic AMP and calcium. The activity of PP-2B is dependent on calcium and calmodulin, while PP-1 is controlled in a variety of ways that depend on the form of the enzyme and the tissue. PP-1 can be inhibited by cyclic AMP in a variety of cells through the A-kinase-catalyzed phosphorylation of inhibitor-1 and its isoforms. Phosphorylation of the glycogen-binding subunit of PP-1G by A-kinase promotes translocation of the catalytic subunit from glycogen particles to cytosol in skeletal muscle, inhibiting the dephosphorylation of glycogen-metabolizing enzymes. Allosteric inhibition of hepatic PP-1G by phosphorylase a occurs in response to signals that elevate cyclic AMP or calcium, and prevents the activation of glycogen synthase in liver. PP-1 can also be activated indirectly by calcium through the ability of PP-2B to dephosphorylate inhibitor-1. This control mechanism may operate in dopaminoceptive neurones of the brain and other cells. The inactive cytosolic form of PP-1 (PP-1I) can be activated in vitro through the glycogen synthase kinase-3-catalyzed phosphorylation of its inhibitory subunit (inhibitor-2), but the physiological significance is unclear.(ABSTRACT TRUNCATED AT 400 WORDS) | lld:pubmed |
| pubmed-article:2549856 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2549856 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2549856 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:2549856 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2549856 | pubmed:issn | 0066-4154 | lld:pubmed |
| pubmed-article:2549856 | pubmed:author | pubmed-author:CohenPP | lld:pubmed |
| pubmed-article:2549856 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2549856 | pubmed:volume | 58 | lld:pubmed |
| pubmed-article:2549856 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2549856 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2549856 | pubmed:pagination | 453-508 | lld:pubmed |
| pubmed-article:2549856 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
| pubmed-article:2549856 | pubmed:meshHeading | pubmed-meshheading:2549856-... | lld:pubmed |
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| pubmed-article:2549856 | pubmed:meshHeading | pubmed-meshheading:2549856-... | lld:pubmed |
| pubmed-article:2549856 | pubmed:year | 1989 | lld:pubmed |
| pubmed-article:2549856 | pubmed:articleTitle | The structure and regulation of protein phosphatases. | lld:pubmed |
| pubmed-article:2549856 | pubmed:affiliation | Department of Biochemistry, University of Dundee, Scotland. | lld:pubmed |
| pubmed-article:2549856 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2549856 | pubmed:publicationType | Review | lld:pubmed |
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