Abstract
THE superfamily of low molecular mass GTP-binding proteins, for which the ras proteins are prototypes, has been implicated in the regulation of diverse biological activities including protein trafficking, secretion, and cell growth and differentiation1-3. One member of this family, CDC42Hs (originally referred to as Gp or G25K)4,5, seems to be the human homologue of the Saccharomyces cerevisiae cell-division-cycle protein, CDC42Sc (refs 6-9). A second S. cerevisiae protein, CDC24 (ref. 10), which is known from complementation studies to act with CDC42Sc to regulate the development of normal cell shape and the selection of nonrandom budding sites in yeast, contains a region with sequence similarity to the dbl oncogene product11-14. Here we show that dbl specifically catalyses the dissociation of GDP from CDC42Hs and thereby qualifies as a highly selective guanine nucleotide exchange factor for the GTP-binding protein. Although guanine nucleotide exchange activities have been previously described for other members of the Ras-related GTP-binding protein family15-17, this is the first demonstration, to our knowledge, of the involvement of a human oncogenic protein in catalysing exchange activity.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 311-314 |
| Number of pages | 4 |
| Journal | Nature |
| Volume | 354 |
| Issue number | 6351 |
| State | Published - Nov 28 1991 |
| Externally published | Yes |
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Catalysis of guanine nucleotide exchange on the CDC42Hs protein by the dbl oncogene product. / Hart, Matthew J; Eva, Alessandra; Evans, Tony; Aaronson, Stuart A.; Cerione, Richard A.
In: Nature, Vol. 354, No. 6351, 28.11.1991, p. 311-314.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Catalysis of guanine nucleotide exchange on the CDC42Hs protein by the dbl oncogene product
AU - Hart, Matthew J
AU - Eva, Alessandra
AU - Evans, Tony
AU - Aaronson, Stuart A.
AU - Cerione, Richard A.
PY - 1991/11/28
Y1 - 1991/11/28
N2 - THE superfamily of low molecular mass GTP-binding proteins, for which the ras proteins are prototypes, has been implicated in the regulation of diverse biological activities including protein trafficking, secretion, and cell growth and differentiation1-3. One member of this family, CDC42Hs (originally referred to as Gp or G25K)4,5, seems to be the human homologue of the Saccharomyces cerevisiae cell-division-cycle protein, CDC42Sc (refs 6-9). A second S. cerevisiae protein, CDC24 (ref. 10), which is known from complementation studies to act with CDC42Sc to regulate the development of normal cell shape and the selection of nonrandom budding sites in yeast, contains a region with sequence similarity to the dbl oncogene product11-14. Here we show that dbl specifically catalyses the dissociation of GDP from CDC42Hs and thereby qualifies as a highly selective guanine nucleotide exchange factor for the GTP-binding protein. Although guanine nucleotide exchange activities have been previously described for other members of the Ras-related GTP-binding protein family15-17, this is the first demonstration, to our knowledge, of the involvement of a human oncogenic protein in catalysing exchange activity.
AB - THE superfamily of low molecular mass GTP-binding proteins, for which the ras proteins are prototypes, has been implicated in the regulation of diverse biological activities including protein trafficking, secretion, and cell growth and differentiation1-3. One member of this family, CDC42Hs (originally referred to as Gp or G25K)4,5, seems to be the human homologue of the Saccharomyces cerevisiae cell-division-cycle protein, CDC42Sc (refs 6-9). A second S. cerevisiae protein, CDC24 (ref. 10), which is known from complementation studies to act with CDC42Sc to regulate the development of normal cell shape and the selection of nonrandom budding sites in yeast, contains a region with sequence similarity to the dbl oncogene product11-14. Here we show that dbl specifically catalyses the dissociation of GDP from CDC42Hs and thereby qualifies as a highly selective guanine nucleotide exchange factor for the GTP-binding protein. Although guanine nucleotide exchange activities have been previously described for other members of the Ras-related GTP-binding protein family15-17, this is the first demonstration, to our knowledge, of the involvement of a human oncogenic protein in catalysing exchange activity.
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M3 - Article
C2 - 1956381
AN - SCOPUS:0026044409
VL - 354
SP - 311
EP - 314
JO - Nature
JF - Nature
SN - 0028-0836
IS - 6351
ER -