Protein kinase C mu is negatively regulated by 14-3-3 signal transduction proteins (Q28139665)

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object named as

A Hausser

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author name string

P Storz

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G Link

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H Stoll

4

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Y C Liu

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A Altman

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F J Johannes

Journal of Biological Chemistry

8

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language of work or name

English

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publication date

2 April 1999

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published in

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volume

274

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page(s)

9258-64

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issue

14

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cites work

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Selective modulation of protein kinase C-theta during T-cell activation

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14-3-3 proteins: a highly conserved, widespread family of eukaryotic proteins

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14-3-3 proteins. Hot numbers in signal transduction

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Activation-modulated association of 14-3-3 proteins with Cbl in T cells

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14-3-3: modulators of signaling proteins?

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14-3-3sigma is a p53-regulated inhibitor of G2/M progression

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Interleukin-3-induced phosphorylation of BAD through the protein kinase Akt

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Akt phosphorylation of BAD couples survival signals to the cell-intrinsic death machinery

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Serine phosphorylation of death agonist BAD in response to survival factor results in binding to 14-3-3 not BCL-X(L)

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Direct interaction between protein kinase C theta (PKC theta) and 14-3-3 tau in T cells: 14-3-3 overexpression results in inhibition of PKC theta translocation and function

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Protein kinase C mu is located at the Golgi compartment

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Protein kinase C mu (PKC mu) associates with the B cell antigen receptor complex and regulates lymphocyte signaling

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The product of par-4, a gene induced during apoptosis, interacts selectively with the atypical isoforms of protein kinase C

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Lambda-interacting protein, a novel protein that specifically interacts with the zinc finger domain of the atypical protein kinase C isotype lambda/iota and stimulates its kinase activity in vitro and in vivo

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14-3-3 inhibits the Dictyostelium myosin II heavy-chain-specific protein kinase C activity by a direct interaction: identification of the 14-3-3 binding domain

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Identification of 14-3-3 proteins in human platelets: effects of synthetic peptides on protein kinase C activation

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