A draft of the human septin interactome

Autor: Marcos Rodrigo Alborghetti, Richard Charles Garratt, Thiago V. Seraphim, Nilson Ivo Tonin Zanchin, Julio C.P. Damalio, João Alexandre Ribeiro Gonçalves Barbosa, J. N. A. Macedo, Eliana M. Assmann, Tatiana de Arruda Campos Brasil de Souza, Jörg Kobarg, Marcel Nakahira, Ana Paula Ulian de Araújo, Luis Fernando Reyes, Nayara S. Cavalcante
Rok vydání: 2010
Předmět:
Zdroj: Repositório Institucional da USP (Biblioteca Digital da Produção Intelectual)
Universidade de São Paulo (USP)
instacron:USP
PLoS ONE, Vol 5, Iss 11, p e13799 (2010)
PLoS ONE
Popis: Background Septins belong to the GTPase superclass of proteins and have been functionally implicated in cytokinesis and the maintenance of cellular morphology. They are found in all eukaryotes, except in plants. In mammals, 14 septins have been described that can be divided into four groups. It has been shown that mammalian septins can engage in homo- and heterooligomeric assemblies, in the form of filaments, which have as a basic unit a hetero-trimeric core. In addition, it has been speculated that the septin filaments may serve as scaffolds for the recruitment of additional proteins. Methodology/Principal Findings Here, we performed yeast two-hybrid screens with human septins 1–10, which include representatives of all four septin groups. Among the interactors detected, we found predominantly other septins, confirming the tendency of septins to engage in the formation of homo- and heteropolymeric filaments. Conclusions/Significance If we take as reference the reported arrangement of the septins 2, 6 and 7 within the heterofilament, (7-6-2-2-6-7), we note that the majority of the observed interactions respect the “group rule”, i.e. members of the same group (e.g. 6, 8, 10 and 11) can replace each other in the specific position along the heterofilament. Septins of the SEPT6 group preferentially interacted with septins of the SEPT2 group (p
Databáze: OpenAIRE