(Q24310359)

2

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Taiping Shi

3

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Bingfeng Lv

4

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Qihua He

5

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Yanfei Zhang

6

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Ting Li

7

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Yingmei Zhang

8

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Quansheng Song

9

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Lu Wang

10

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Dalong Ma

Bcr and Raf form a complex in vivo via 14-3-3 proteins.

11

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language of work or name

English

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publication date

December 2008

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published in

Cellular Signalling

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volume

20

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issue

12

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page(s)

2208-20

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cites work

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The novel protein PTPIP51 exhibits tissue- and cell-specific expression

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Protein tyrosine phosphatase interacting protein 51 (PTPIP51) is a novel mitochondria protein with an N-terminal mitochondrial targeting sequence and induces apoptosis

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Threshold levels of ERK activation for chemotactic migration differ for NGF and EGF in rat pheochromocytoma PC12 cells

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A brake becomes an accelerator: PTP1B--a new therapeutic target for breast cancer.

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Regulation of Raf-1 by direct feedback phosphorylation.

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How do 14-3-3 proteins work?-- Gatekeeper phosphorylation and the molecular anvil hypothesis

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The structural basis for 14-3-3:phosphopeptide binding specificity

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Interaction of 14-3-3 with signaling proteins is mediated by the recognition of phosphoserine

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Bcl-2 targets the protein kinase Raf-1 to mitochondria

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14-3-3 dimers probe the assembly status of multimeric membrane proteins

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Structural analysis of 14-3-3 phosphopeptide complexes identifies a dual role for the nuclear export signal of 14-3-3 in ligand binding

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Large-scale mapping of human protein-protein interactions by mass spectrometry

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Negative regulation of EGFR signalling through integrin-alpha1beta1-mediated activation of protein tyrosine phosphatase TCPTP

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Prohibitin is required for Ras-induced Raf-MEK-ERK activation and epithelial cell migration

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Protein tyrosine phosphatase 1B deficiency or inhibition delays ErbB2-induced mammary tumorigenesis and protects from lung metastasis

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The RAF proteins take centre stage

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Imaging of cell migration

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14-3-3 zeta negatively regulates raf-1 activity by interactions with the Raf-1 cysteine-rich domain

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The dominant negative Ras mutant, N17Ras, can inhibit signaling independently of blocking Ras activation

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Protein kinase A blocks Raf-1 activity by stimulating 14-3-3 binding and blocking Raf-1 interaction with Ras.

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14-3-3 acts as an intramolecular bridge to regulate cdc25B localization and activity

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14-3-3 proteins: active cofactors in cellular regulation by serine/threonine phosphorylation

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Mechanism in the sequential control of cell morphology and S phase entry by epidermal growth factor involves distinct MEK/ERK activations

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Identification of Raf-1 S471 as a novel phosphorylation site critical for Raf-1 and B-Raf kinase activities and for MEK binding

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The MAPK signaling cascade

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Mitogen-activated protein kinase pathways mediated by ERK, JNK, and p38 protein kinases

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Association of the protein kinases c-Bcr and Bcr-Abl with proteins of the 14-3-3 family

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Negative regulation of Raf-1 by phosphorylation of serine 621.

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