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Microtubule Polymerase and Processive Plus-end Tracking Functions Originate from Distinct Features Within TOG Domain Arrays
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| 자료유형 | 학위논문 |
|---|---|
| 서명/저자사항 | Microtubule Polymerase and Processive Plus-end Tracking Functions Originate from Distinct Features Within TOG Domain Arrays. |
| 개인저자 | Cook, Brian Douglas. |
| 단체저자명 | University of California, Davis. Biochemistry Molecular Cellular and Developmental Biology. |
| 발행사항 | [S.l.]: University of California, Davis., 2019. |
| 발행사항 | Ann Arbor: ProQuest Dissertations & Theses, 2019. |
| 형태사항 | 168 p. |
| 기본자료 저록 | Dissertations Abstracts International 81-04B. Dissertation Abstract International |
| ISBN | 9781085798358 |
| 학위논문주기 | Thesis (Ph.D.)--University of California, Davis, 2019. |
| 일반주기 |
Source: Dissertations Abstracts International, Volume: 81-04, Section: B.
Advisor: Al-Bassam, Jawdat. |
| 이용제한사항 | This item must not be sold to any third party vendors.This item must not be added to any third party search indexes. |
| 요약 | Microtubules (MT) are dynamic protein polymers that form tubular structures that grow through the addition of 慣棺-tubulin heterodimers to the ends. Most growth occurs at one end of the MT and the cell has evolved many protein regulators to control the many different aspects of MTs dynamics at this region. One family of vital MT regulators are the XMAP215/Stu2/Alp14 proteins that accelerate MT plus-end polymerization by recruiting 慣棺-tubulin dimers while processively tracking the growing MT end via arrays of Tumor Overexpressed Gene (TOG) domains. These proteins are found throughout eukaryotes and critical for many cellular functions. It remains poorly understood how MT polymerization and MT plus-end tracking functions arise from 慣棺-tubulin recruitment, mediated by the distinct TOG1 and TOG2 domains, and the organization of these arrays into higher ordered assemblies.This thesis focuses on determining the molecular mechanism of MT polymerization by a XMAP215/Stu2/Alp14 family member. Chapter 1 provides an overview of MTs and the proteins that associate with them. The second chapter of this thesis describes structural and biochemical studies to explain the high order organization of these proteins. These studies present a clear model for how XMAP215/Stu2/Alp14 proteins accelerate MT polymerization. Chapter 3 focuses on testing the model presented in chapter 2 by using a combination of in vivo and in vitro studies. The final chapter provides a summary of the chapters, concluding remarks, and plans for future studies. |
| 일반주제명 | Biochemistry. Physiology. Cellular biology. Health sciences. Molecular biology. |
| 언어 | 영어 |
| 바로가기 | 
: 이 자료의 원문은 한국교육학술정보원에서 제공합니다. |
