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|Title:||Regulation of Sla2p by activity in endocytosis and actin organization by the Ark1/Prk1 family of kinases||Authors:||NEEYOR BOSE||Keywords:||actin endocytosis Sla2p phosphorylation C-terminus||Issue Date:||25-Aug-2009||Citation:||NEEYOR BOSE (2009-08-25). Regulation of Sla2p by activity in endocytosis and actin organization by the Ark1/Prk1 family of kinases. ScholarBank@NUS Repository.||Abstract:||Sla2p is an adaptor molecule involved in endocytosis and actin organization in S.cerevisiae whose deletion causes accumulation of actin at the cortex and block in endocytosis. Sla2p is phosphorylated by Prk1p and Ark1p kinases which regulate actin organization and endocytosis in yeast. Constitutive phosphorylation on Sla2p causes longer lifespan at the cortex, endocytic defects and changes Sla2pb s affinity for Scd5p and Pan1p. Sla2p is dephosphorylated by Scd5p/Glc7p complex. C-terminal of Sla2p contains two coiled-coil domains and F-actin binding THATCH domain. The second coiled-coil domain (700- 730 a.a) is vital for interactions with Ark1p and Scd5p. Deletion of this domain causes temperature sensitivity, actin aberrations and block in endocytosis. Systematic truncations in the C-terminal region of Sla2p revealed the strongest phenotype was obtained by deleting just the second coiled-coil domain (sla2o CC mutant). High-copy suppressor screening found that overexpressing Abp1p rescues the temperature sensitivity of sla2o CC, actin aberrations and endocytic defects.||URI:||http://scholarbank.nus.edu.sg/handle/10635/21801|
|Appears in Collections:||Ph.D Theses (Open)|
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