{"id":{"repo_id":"nus","oai_identifier":"oai:scholarbank.nus.edu.sg:10635/23181"},"canonical_url":"https://search.dev.ndltd.org/etd/nus/oai:scholarbank.nus.edu.sg:10635/23181","repository":{"repo_id":"nus","name":"National University of Singapore","base_url":"https://scholarbank.nus.edu.sg/oai/request"},"display":{"title":"Functional analysis of syp1, a novel substrate of the serine/threonine kinase prk1","abstract":"In budding yeast, the actin and septin cytoskeletons are important for the establishment of cell polarity. During the cell cycle, these cytoskeletons undergo dramatic reorganization which is regulated by many cytoskeleton-associated proteins. In this study, Syp1p has been found to have functional interactions with the actin cytoskeleton. Syp1p is a new substrate of Prk1p, a kinase that regulates actin dynamics. Syp1p colocalizes with actin cytoskeleton whose integrity is required for the polarized localization of Syp1p. Syp1p can physically interact with the actin-associated protein Sla1p. Furthermore, Syp1p overexpression suppresses the defects of BNI1 deletion mutant. In addition to its roles in actin cytoskeleton, Syp1p is also discovered to be a new regulator of the septin dynamics. Syp1p colocalizes and physically interacts with septins. Syp1p overexpression disorganizes septin structure and induces the Swe1p-dependent elongated bud phenotype. Syp1p also regulates the organization of septins in different cell cycle stages.","abstract_html":"In budding yeast, the actin and septin cytoskeletons are important for the establishment of cell polarity. During the cell cycle, these cytoskeletons undergo dramatic reorganization which is regulated by many cytoskeleton-associated proteins. In this study, Syp1p has been found to have functional interactions with the actin cytoskeleton. Syp1p is a new substrate of Prk1p, a kinase that regulates actin dynamics. Syp1p colocalizes with actin cytoskeleton whose integrity is required for the polarized localization of Syp1p. Syp1p can physically interact with the actin-associated protein Sla1p. Furthermore, Syp1p overexpression suppresses the defects of BNI1 deletion mutant. In addition to its roles in actin cytoskeleton, Syp1p is also discovered to be a new regulator of the septin dynamics. Syp1p colocalizes and physically interacts with septins. Syp1p overexpression disorganizes septin structure and induces the Swe1p-dependent elongated bud phenotype. Syp1p also regulates the organization of septins in different cell cycle stages.","abstract_has_math":false,"creators":["QIU WENJIE"],"institution":null,"degree_name":null,"degree_level":null,"degree_discipline":null,"degree_department":null,"school":null,"contributors":[],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2007,"date_issued":"2007-10-30","date_published":"2007-10-30","updated_at":"2026-07-24T03:30:47Z","subjects":["actin, septin, Syp1p, Prk1p, cell division, cytokinesis"],"languages":[],"rights":[],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":null,"outbound_label":null,"outbound_source":null},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:creator","label":"Author","values":["QIU WENJIE"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date.issued","label":"Date","values":["2007-10-30"]},{"key":"dc:relation.isreferencedby","label":"Dc Relation Isreferencedby","values":["https://scholarbank.nus.edu.sg/handle/10635/23181"]},{"key":"dc:type","label":"Dc Type","values":["Thesis"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["actin, septin, Syp1p, Prk1p, cell division, cytokinesis"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier.uri","label":"Identifier URI","values":["https://scholarbank.nus.edu.sg/bitstreams/820c4bf7-63a6-4399-87df-83981779cf2d/download"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["In budding yeast, the actin and septin cytoskeletons are important for the establishment of cell polarity. 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