Biomedical subjects

P Sivadon

Publications and source records attributed to P Sivadon.

At least 19 recordsLinked to original sources

PubMed1997

Functional assessment of the yeast Rvs161 and Rvs167 protein domains.

Mutations in RVS161 and RVS167 yeast genes induce identical phenotypes associated to actin cytoskeleton disorders. The whole Rvs161 protein is similar to the amino-terminal part of Rvs167p, thus defining a RVS domain. In addition to this domain, Rvs167p contains a central glycine-proline-alanine rich domain and a SH3 domain. To assess the function of these different domains we have expressed recombinant Rvs proteins in rvs mutant strains. Phenotype analysis has shown that the RVS and SH3 domains are necessary for phenotypical complementation, whereas the GPA domain is not. Moreover, we have demonstrated that the RVS domains from Rvs161p and Rvs167p have distinct roles, and that the SH3 domain needs the specific RVS domain of Rvs167p to function. These results suggest that Rvs161p and Rvs167p play distinct roles, while acting together in a common function.

Actins↗

PubMed1997

Cloning of the multicopy suppressor gene SUR7: evidence for a functional relationship between the yeast actin-binding protein Rvs167 and a putative membranous protein.

The rvs161 and rvs167 mutant cells exhibit several identical phenotypes including sensitivity to several different growth conditions and morphological defects such as alteration of the actin cytoskeleton and budding patterns. The selection of genes that, when overexpressed, are able to suppress the reduced viability upon carbon starvation of the rvs167 mutant strain, has allowed the cloning of the SUR7 gene (Accession Number Z46729x11). We showed that the suppressive ability of the overexpressed SUR7 gene concerns all the rvs167 phenotypes. However, this suppression is only partial since the rvs167-suppressed strain is not of wild-type phenotype. Moreover, SUR7 is also able to suppress partially the phenotypes exhibited by the rvs161 and rvs167 and rvs161 mutant strains. The SUR7 gene encodes a putative integral membrane protein with four transmembrane domains. Furthermore, sequence comparisons revealed that Sur7p and two other proteins, Yn1194p and Yd1222p, present significant sequence and structural similarities. Taken together, these results strongly suggest that the Rvs161 and Rvs167 proteins act together in relation with Sur7p. Moreover, the putative transmembranous character of Sur7p suggests a membrane localization of the Rvs function, a localization which is consistent with the different rvs phenotypes and the actin-Rvs167p interaction.

Actins↗

PubMed1995

Actin cytoskeleton and budding pattern are altered in the yeast rvs161 mutant: the Rvs161 protein shares common domains with the brain protein amphiphysin.

The actin cytoskeleton cells is altered in rvs161 mutant yeast, with the defect becoming more pronounced under unfavorable growth conditions, as described for the rvs167 mutant. The cytoskeletal alteration has no apparent effect on invertase secretion and polarized growth. Mutations in RVS161, just as in RVS167, lead to a random budding pattern in a/alpha diploid cells. This behavior is not observed in a/a diploid cells homozygous for the rvs161-1 or rvs167-1 mutations. In addition, sequence comparisons revealed that amphiphysin, a protein first found in synaptic vesicles of chicken and shown to be the autoantigen of Stiff Man syndrome, presents similarity with both Rvs proteins. Furthermore, limited similarities with myosin heavy chain and tropomyosin alpha chain from higher eukaryotic cells allow for the definition of a possible consensus sequence. The finding of related sequences suggests the existence of a function for these proteins that is conserved among eukaryotic organisms.

Actins↗

PubMed1981