Mutational analysis of Raf-1 cysteine rich domain: requirement for a cluster of basic aminoacids for interaction with phosphatidylserine. (Q38320200)

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31 October 2019

title

Mutational analysis of Raf-1 cysteine rich domain: requirement for a cluster of basic aminoacids for interaction with phosphatidylserine (English)

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31 October 2019

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2

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31 October 2019

author name string

T Improta-Brears

series ordinal

1

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31 October 2019

R M Bell

series ordinal

3

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31 October 2019

publication date

1 August 1999

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Molecular and Cellular Biochemistry

31 October 2019

published in

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31 October 2019

volume

198

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31 October 2019

issue

1-2

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31 October 2019

page(s)

171-178

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https://scigraph.springernature.com/pub.10.1023/a:1006981411691

31 October 2019

exact match

0 references

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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

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14-3-3: modulators of signaling proteins?

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Requirement for Ras in Raf activation is overcome by targeting Raf to the plasma membrane

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The native structure of the activated Raf protein kinase is a membrane-bound multi-subunit complex

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The solution structure of the Raf-1 cysteine-rich domain: a novel ras and phospholipid binding site

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Transcription factor ISGF-3 formation requires phosphorylated Stat91 protein, but Stat113 protein is phosphorylated independently of Stat91 protein

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A signal chain of events

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Two distinct Raf domains mediate interaction with Ras

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Normal and oncogenic p21ras proteins bind to the amino-terminal regulatory domain of c-Raf-1

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Regulation of Raf-1 and Raf-1 mutants by Ras-dependent and Ras-independent mechanisms in vitro

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The cysteine-rich region of raf-1 kinase contains zinc, translocates to liposomes, and is adjacent to a segment that binds GTP-ras.

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Mutagenesis of the H-ras p21 at glycine-60 residue disrupts GTP-induced conformational change

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Immunocytochemical localization of eight protein kinase C isozymes overexpressed in NIH 3T3 fibroblasts. Isoform-specific association with microfilaments, Golgi, endoplasmic reticulum, and nuclear and cell membranes

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A phorbol ester binding domain of protein kinase C gamma. Deletion analysis of the Cys2 domain defines a minimal 43-amino acid peptide

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Complexes of Ras.GTP with Raf-1 and mitogen-activated protein kinase kinase

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Crystal structure of the cys2 activator-binding domain of protein kinase C delta in complex with phorbol ester

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Ras interaction with two distinct binding domains in Raf-1 may be required for Ras transformation

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Raf-1 kinase possesses distinct binding domains for phosphatidylserine and phosphatidic acid. Phosphatidic acid regulates the translocation of Raf-1 in 12-O-tetradecanoylphorbol-13-acetate-stimulated Madin-Darby canine kidney cells

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Raf-1 activates MAP kinase-kinase

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Activation and substrate specificity of the human protein kinase C alpha and zeta isoenzymes

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Mammalian Ras interacts directly with the serine/threonine kinase Raf

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Identification of discrete segments of human Raf-1 kinase critical for high affinity binding to Ha-Ras.

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Protein kinase C activation in mixed micelles. Mechanistic implications of phospholipid, diacylglycerol, and calcium interdependencies.

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Chemical specificity and physical properties of the lipid bilayer in the regulation of protein kinase C by anionic phospholipids: evidence for the lack of a specific binding site for phosphatidylserine

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Raf meets Ras: completing the framework of a signal transduction pathway

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A single amino acid change in Raf-1 inhibits Ras binding and alters Raf-1 function

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Binding of 14-3-3 proteins to the protein kinase Raf and effects on its activation

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The complete coding sequence of the human A-raf-1 oncogene and transforming activity of a human A-raf carrying retrovirus

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

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