Rab5 Activation by the Vps9 Domain

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dc.contributor.advisor Horazdovsky , Bruce en
dc.creator Carney , Darren Scott en
dc.date.accessioned 2010 -07 -12T17 :18 :35Z en
dc.date.accessioned 2014 -02 -19T22 :01 :29Z
dc.date.available 2010 -07 -12T17 :18 :35Z en
dc.date.available 2014 -02 -19T22 :01 :29Z
dc.date.issued 2007 -05 -21 en
dc.identifier.other en
dc.identifier.uri http : / /hdl .handle .net /2152 .5 /252 en
dc.description.abstract The movement of proteins through the endocytic pathway is a complex and highly regulated process . Not only is this pathway used to internalize cellular nutrients , but it is also used to modulate a cell's response to extracellular stimuli . Internalization and subsequent trafficking of transmembrane receptor proteins that receive these signals from the external milieu play an essential role in establishing and maintaining cellular homeostasis . As key regulators of the early stages the endocytic pathway , the small GTPases of the Rab5 family serve an essential function in integrating intracellular protein traffic and these cell signaling events . Rab5 proteins exert their influence on protein trafficking only when bound to GTP . A large family of proteins containing a conserved domain (Vps9 ) activate Rab5 by promoting the release of GDP and reloading of GTP . These nucleotide exchange factors contain additional domains which link them to specific cellular locations or signaling cascades . The multiplicity of these Rab5 proteins and exchange factors raises the question of how these proteins specifically interact to regulate individual trafficking events . To investigate this specificity , the three Rab5 proteins of Saccharomyces cerevisiae , Vps21 , Ypt52 and Ypt53 , and the two yeast Vps9 domain -containing proteins , Vps9 and Muk1 , were analyzed . This analysis identified previously unappreciated roles for Ypt53 and Muk1 in a relatively late stage of endocytosis . A mutational analysis of Vps9 identified several residues important for Vps9 domain function and shed light on a possible intramolecular regulation of this domain by the carboxy -terminal ubiquitin -binding CUE domain . Finally , structural studies of the Rab5 /Vps9 domain complex were initiated to gain a better understanding of the molecular mechanisms by which Rab5 proteins interact with and are activated by the Vps9 domain . en
dc.format.medium Electronic en
dc.format.mimetype application /pdf en
dc.language.iso en en
dc.subject Protein Transport en
dc.subject Endocytosis en
dc.subject rab5 GTP -Binding Proteins en
dc.title Rab5 Activation by the Vps9 Domain en
dc.type.genre dissertation en
dc.type.material Text en
thesis.degree.name Doctor of Philosophy en
thesis.degree.level Ph .D . en
thesis.degree.discipline Biological Chemistry en
thesis.degree.grantor Graduate School of Biomedical Sciences en
thesis.degree.department en
dc.format.digitalOrigin born digital en
thesis.date.available 2008 -05 -21 en


Rab5 Activation by the Vps9 Domain. Graduate School of Biomedical Sciences. Available electronically from http : / /hdl .handle .net /2152 .5 /252 .

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