Endomembrane trafficking of ras: the CAAX motif targets proteins to the ER and Golgi (Q28140190)

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V K Chiu

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J Silletti

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M Feoktistov

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T Morimoto

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D Michaelson

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I E Ivanov

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M R Philips

Modulation of Ras and a-factor function by carboxyl-terminal proteolysis

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publication date

9 July 1999

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language of work or name

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98

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issue

1

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page(s)

69-80

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cites work

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Protein prenyltransferases

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Protein isoprenylation and methylation at carboxyl-terminal cysteine residues

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Endolyn-78, a membrane glycoprotein present in morphologically diverse components of the endosomal and lysosomal compartments: implications for lysosome biogenesis

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Mammalian prenylcysteine carboxyl methyltransferase is in the endoplasmic reticulum

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ATPase and phosphatase activity of Na+,K+-ATPase: molar and specific activity, protein determination

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The precision of ultraviolet absorption measurements in the Schmidt-Thannhauser procedure for nucleic acid estimation

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Isolation and characterization of Golgi membranes from bovine liver

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A novel membrane-associated metalloprotease, Ste24p, is required for the first step of NH2-terminal processing of the yeast a-factor precursor

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The potential of farnesyltransferase inhibitors as cancer chemotherapeutics

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All ras proteins are polyisoprenylated but only some are palmitoylated

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A polybasic domain or palmitoylation is required in addition to the CAAX motif to localize p21ras to the plasma membrane

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A CAAX or a CAAL motif and a second signal are sufficient for plasma membrane targeting of ras proteins.

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

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Rapid redistribution of Golgi proteins into the ER in cells treated with brefeldin A: evidence for membrane cycling from Golgi to ER

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Farnesyl derivatives of rigid carboxylic acids-inhibitors of ras-dependent cell growth

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Significance of C-terminal cysteine modifications to the biological activity of the Saccharomyces cerevisiae a-factor mating pheromone

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Prenylcysteine-directed carboxyl methyltransferase activity in human neutrophil membranes

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Evolutionary biology. Pelvic problems for mammals

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Inhibition of purified p21ras farnesyl:protein transferase by Cys-AAX tetrapeptides

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TheSaccharomyces cerevisiaePrenylcysteine Carboxyl Methyltransferase Ste14p Is in the Endoplasmic Reticulum Membrane

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Nucleotide sequence of the yeast STE14 gene, which encodes farnesylcysteine carboxyl methyltransferase, and demonstration of its essential role in a-factor export

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Endoplasmic reticulum membrane localization of Rce1p and Ste24p, yeast proteases involved in carboxyl-terminal CAAX protein processing and amino-terminal a-factor cleavage

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Fluorimetric evaluation of the affinities of isoprenylated peptides for lipid bilayers

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

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Metabolic turnover of human c-rasH p21 protein of EJ bladder carcinoma and its normal cellular and viral homologs

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Rapid plasma membrane anchoring of newly synthesized p59fyn: selective requirement for NH2-terminal myristoylation and palmitoylation at cysteine-3.

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Localization of the src gene product of the Harvey strain of MSV to plasma membrane of transformed cells by electron microscopic immunocytochemistry

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Identifiers

DOI

1 reference

Consolidated OpenCitations Corpus – April 2017

1 reference

Consolidated OpenCitations Corpus – April 2017

PubMed publication ID

10412982

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Consolidated OpenCitations Corpus – April 2017