Insulin controls subcellular localization and multisite phosphorylation of the phosphatidic acid phosphatase, lipin 1.

Insulin controls subcellular localization and multisite phosphorylation of the phosphatidic acid phosphatase, lipin 1. Research Abstract Details 

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Insulin controls subcellular localization and multisite phosphorylation of the phosphatidic acid phosphatase, lipin 1. Abstract Text:

Thurl E Harris,Todd A Huffman,An Chi,Jeffrey Shabanowitz,Donald F Hunt,Anil Kumar,John C Lawrence,

Brain, liver, kidney, heart, and skeletal muscle from fatty liver dystrophy (fld/fld) mice, which do not express lipin 1 (lipin), contained much less Mg(2+)-dependent phosphatidic acid phosphatase (PAP) activity than tissues from wild type mice. Lipin harboring the fld(2j) (Gly(84) --> Arg) mutation exhibited relatively little PAP activity. These results indicate that lipin is a major PAP in vivo and that the loss of PAP activity contributes to the fld phenotype. PAP activity was readily detected in immune complexes of lipin from 3T3-L1 adipocytes, where the protein was found both as a microsomal form and a soluble, more highly phosphorylated, form. Fifteen phosphorylation sites were identified by mass spectrometric analyses. Insulin increased the phosphorylation of multiple sites and promoted a gel shift that was due in part to phosphorylation of Ser(106). In contrast, epinephrine and oleic acid promoted dephosphorylation of lipin. The PAP-specific activity of lipin was not affected by the hormones or by dephosphorylation of lipin with protein phosphatase 1. However, the ratio of soluble to microsomal lipin was markedly increased in response to insulin and decreased in response to epinephrine and oleic acid. The results suggest that insulin and epinephrine control lipin primarily by changing localization rather than intrinsic PAP activity.

Insulin controls subcellular localization and multisite phosphorylation of the phosphatidic acid phosphatase, lipin 1. Publishing Authors By Initials

TE Harris,TA Huffman,A Chi,J Shabanowitz,DF Hunt,A Kumar,JC Lawrence,

For similar biochemical phenomena, metabolism, and nutrition: biochemical phenomena: protein binding research abstracts see: biochemical phenomena, metabolism, and nutrition: biochemical phenomena: protein binding research

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Insulin controls subcellular localization and multisite phosphorylation of the phosphatidic acid phosphatase, lipin 1. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: The Journal of biological chemistry

VOLUME: 282

Page Numbers: 277-86

Journal Abbreviation: J. Biol. Chem.

ISSN: 0021-9258

DAY: 14

MONTH: 11

YEAR: 2006

Insulin controls subcellular localization and multisite phosphorylation of the phosphatidic acid phosphatase, lipin 1. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 2985121

Insulin controls subcellular localization and multisite phosphorylation of the phosphatidic acid phosphatase, lipin 1. Keywords Mesh Terms:

KEYWORDS: Protein Binding

MESH TERMS: chemistry

Chemical & Substance for Abstract: Insulin controls subcellular localization and multisite phosphorylation of the phosphatidic acid phosphatase, lipin 1. Information

Substance Name: Arginine

Registry Number: 74-79-3

Grant and Affiliation Information for Insulin controls subcellular localization and multisite phosphorylation of the phosphatidic acid phosphatase, lipin 1.

AFFILIATION: Department of Pharmacology, University of Virginia, Charlottesville, Virginia 22908-0735, USA.

Country: United States

AGENCY: United States NIGMS

GRANT: GM37573

ACRONYM: GM

MEDLINETA: J Biol Chem

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