Alternative splicing of the human proto-oncogene c-H-ras renders a new Ras family protein that trafficks to cytoplasm and nucleus

We characterized a novel protein of the Ras family, p19 (H-RasIDX). The c-H-ras proto-oncogene undergoes alternative splicing of the exon termed IDX. We show that the alternative p19 mRNA is stable and as abundant as p21 (p21 H-Ras4A) mRNA in all of the human tissues and cell lines tested. IDX is sp...

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Bibliographic Details
Published in:Cancer research (Chicago, Ill.) Ill.), 2003-09, Vol.63 (17), p.5178-5187
Main Authors: GUIL, Sonia, DE LA IGLESIA, Nana, FERNANDEZ-LARREA, Juan, CIFUENTES, Daniel, FERRER, Juan C, GUINOVART, Joan J, BACH-ELIAS, Montse
Format: Article
Language:English
Subjects:
3T3 Cells
Alternative Splicing
Animals
Base Sequence
Biological and medical sciences
Cell Nucleus - metabolism
Cell physiology
Cell transformation and carcinogenesis. Action of oncogenes and antioncogenes
Consensus Sequence
COS Cells
Cytoplasm - metabolism
Fundamental and applied biological sciences. Psychology
Genes, ras - genetics
GTP-Binding Proteins
HeLa Cells
Humans
Mice
Molecular and cellular biology
Molecular Sequence Data
Neoplasm Proteins - metabolism
Protein Isoforms
Rabbits
ras Proteins - biosynthesis
ras Proteins - genetics
ras Proteins - metabolism
Rats
Receptors for Activated C Kinase
Receptors, Cell Surface
RNA, Messenger - genetics
RNA, Messenger - metabolism
Sequence Homology, Amino Acid
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Summary:We characterized a novel protein of the Ras family, p19 (H-RasIDX). The c-H-ras proto-oncogene undergoes alternative splicing of the exon termed IDX. We show that the alternative p19 mRNA is stable and as abundant as p21 (p21 H-Ras4A) mRNA in all of the human tissues and cell lines tested. IDX is spliced into stable mRNA in different mammalian species, which present a high degree of nucleotide conservation. Both the endogenous and the transiently expressed p19 protein are detected in COS-1 and HeLa cells and show nuclear diffuse and speckled patterns as well as cytoplasmic localization. In yeast two-hybrid assays, p19 did not interact with two known p21 effectors, Raf1 and Rin1, but was shown to interact with RACK1, a scaffolding protein that promotes multiprotein complexes in different signaling pathways. This observation suggests that p19 and p21 play differential and complementary roles in the cell.
ISSN:0008-5472
1538-7445