Prenylated Rab acceptor protein is a receptor for prenylated small GTPases (Q24291200)

Journal of Biological Chemistry

GOA release 2020-03-11

author name string

C Figueroa

series ordinal

1

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J Taylor

series ordinal

2

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A B Vojtek

series ordinal

3

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language of work or name

English

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publication date

27 July 2001

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published in

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volume

276

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page(s)

28219-25

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issue

30

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cites work

Interaction cloning and characterization of the cDNA encoding the human prenylated rab acceptor (PRA1).

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All ras proteins are polyisoprenylated but only some are palmitoylated

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Mammalian Ras interacts directly with the serine/threonine kinase Raf

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Reticulocyte lysate assay for in vitro translation and posttranslational modification of Ras proteins

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New insights into the interaction of Ras with the plasma membrane

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Endomembrane trafficking of ras: the CAAX motif targets proteins to the ER and Golgi

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Piccolo, a presynaptic zinc finger protein structurally related to bassoon

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The GTPase superfamily: conserved structure and molecular mechanism

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Genomic analysis of metastasis reveals an essential role for RhoC

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LKB1, a novel serine/threonine protein kinase and potential tumour suppressor, is phosphorylated by cAMP-dependent protein kinase (PKA) and prenylated in vivo

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Isoprenoid addition to Ras protein is the critical modification for its membrane association and transforming activity

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Ras membrane targeting is essential for glucose signaling but not for viability in yeast

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Two-hybrid system screen with the small GTP-binding protein Rab6. Identification of a novel mouse GDP dissociation inhibitor isoform and two other potential partners of Rab6

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p110delta, a novel phosphatidylinositol 3-kinase catalytic subunit that associates with p85 and is expressed predominantly in leukocytes

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Isolation and characterization of a dual prenylated Rab and VAMP2 receptor

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Prenylation-dependent association of Ki-Ras with microtubules. Evidence for a role in subcellular trafficking

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Increasing complexity of the Ras signaling pathway.

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A non-farnesylated Ha-Ras protein can be palmitoylated and trigger potent differentiation and transformation

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RhoA prenylation is required for promotion of cell growth and transformation and cytoskeleton organization but not for induction of serum response element transcription.

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The C-terminal polylysine region and methylation of K-Ras are critical for the interaction between K-Ras and microtubules

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PRA1 inhibits the extraction of membrane-bound rab GTPase by GDI1.

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Intracellular localization of the P21rho proteins

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Protein prenylation, et cetera: signal transduction in two dimensions

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The effect of posttranslational modifications on the interaction of Ras2 with adenylyl cyclase

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TC21 causes transformation by Raf-independent signaling pathways

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Erf2, a novel gene product that affects the localization and palmitoylation of Ras2 in Saccharomyces cerevisiae

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H-ras but not K-ras traffics to the plasma membrane through the exocytic pathway

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Protein prenylation: molecular mechanisms and functional consequences

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The potential of farnesyltransferase inhibitors as cancer chemotherapeutics

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Identifiers

DOI

10.1074/JBC.M101763200

1 reference

Fatcat

https://api.fatcat.wiki/v0/release/jqgu33rij5gfjnqcc3kznmhq2m

30 July 2022

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Fatcat ID

release_jqgu33rij5gfjnqcc3kznmhq2m

1 reference

Fatcat

https://api.fatcat.wiki/v0/release/jqgu33rij5gfjnqcc3kznmhq2m

30 July 2022

mapped directly with Wikidata item

1 reference

https://api.fatcat.wiki/v0/release/jqgu33rij5gfjnqcc3kznmhq2m

30 July 2022