dc.creatorNAKAHIRA, Marcel
dc.creatorMACEDO, Joci Neuby Alves
dc.creatorSERAPHIM, Thiago Vargas
dc.creatorCAVALCANTE, Nayara
dc.creatorSOUZA, Tatiana A. C. B.
dc.creatorDAMALIO, Julio Cesar Pissuti
dc.creatorREYES, Luis Fernando
dc.creatorASSMANN, Eliana M.
dc.creatorALBORGHETTI, Marcos R.
dc.creatorGARRATT, Richard Charles
dc.creatorARAUJO, Ana Paula Ulian de
dc.creatorZANCHIN, Nilson I. T.
dc.creatorBARBOSA, Joao A. R. G.
dc.creatorKOBARG, Joerg
dc.date.accessioned2012-04-19T15:36:01Z
dc.date.accessioned2018-07-04T14:42:35Z
dc.date.available2012-04-19T15:36:01Z
dc.date.available2018-07-04T14:42:35Z
dc.date.created2012-04-19T15:36:01Z
dc.date.issued2010
dc.identifierPLOS ONE, v.5, n.11, 2010
dc.identifier1932-6203
dc.identifierhttp://producao.usp.br/handle/BDPI/16537
dc.identifier10.1371/journal.pone.0013799
dc.identifierhttp://dx.doi.org/10.1371/journal.pone.0013799
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1613359
dc.description.abstractBackground: 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<0.001), SEPT3 group (p<0.001) and SEPT7 group (p<0.001). SEPT2 type septins preferentially interacted with septins of the SEPT6 group (p<0.001) aside from being the only septin group which interacted with members of its own group. Finally, septins of the SEPT3 group interacted preferentially with septins of the SEPT7 group (p<0.001). Furthermore, we found non-septin interactors which can be functionally attributed to a variety of different cellular activities, including: ubiquitin/sumoylation cycles, microtubular transport and motor activities, cell division and the cell cycle, cell motility, protein phosphorylation/signaling, endocytosis, and apoptosis.
dc.languageeng
dc.publisherPUBLIC LIBRARY SCIENCE
dc.relationPlos One
dc.rightsCopyright PUBLIC LIBRARY SCIENCE
dc.rightsopenAccess
dc.titleA Draft of the Human Septin Interactome
dc.typeArtículos de revistas


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