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Cooperative Functions of the Retrograde Vesicle Fusion Machinery
Cooperative Functions of the Retrograde Vesicle Fusion Machinery
상세정보
- 자료유형
- 학위논문 서양
- 최종처리일시
- 20250211150930
- ISBN
- 9798382193038
- DDC
- 574
- 서명/저자
- Cooperative Functions of the Retrograde Vesicle Fusion Machinery
- 발행사항
- [Sl] : Princeton University, 2024
- 발행사항
- Ann Arbor : ProQuest Dissertations & Theses, 2024
- 형태사항
- 109 p
- 주기사항
- Source: Dissertations Abstracts International, Volume: 85-10, Section: B.
- 주기사항
- Includes supplementary digital materials.
- 주기사항
- Advisor: Hughson, Frederick M.
- 학위논문주기
- Thesis (Ph.D.)--Princeton University, 2024.
- 초록/해제
- 요약N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs) mediate most intracellular membrane fusion events. SNAREs from apposed membranes interact to form membrane-bridging complexes that pull the membranes together, leading to lipid mixing and fusion. While SNAREs alone can drive membrane fusion, they are insufficient to fuse membranes at physiologically relevant speeds. To accelerate the process, membrane tethering complexes (MTC) mediate an initial attachment between a vesicle and a target membrane, and Sec1/Munc18 (SM) proteins accelerate the SNARE assembly step. How these families of proteins cooperate in vesicle capture and fusion, however, is poorly understood. Here, we present two structures of the Golgi-endoplasmic reticulum (ER) retrograde pathway fusion machinery. The first structure, the Saccharomyces cerevisiae Dsl1 MTC bound to the ER SNAREs Sec20 and Use1, is the first reported structure of a tethering complex engaged with other fusion machinery. Together, the trimeric Dsl1 complex and SNAREs form a rigid heteropentamer, the assembly of which is essential for yeast viability. This complex also bears unexpected similarities to the much-larger MTC exocyst, suggesting possible principles of MTC function. The second structure, the SM protein Sly1 bound to the ER SNARE Ufe1, constitutes the remainder of the ER-associated fusion machinery. The remaining Golgi-ER SNARE, Sec22, is embedded in and contributed by the Golgi-derived vesicle. Both the Dsl1 complex and Sly1 remain stably associated with SNAREs during SNARE assembly, resulting in an octameric supercomplex. Our data support a model in which the Dsl1 complex and Sly1 collaborate to localize SNAREs at the site of fusion and drive SNARE assembly and membrane fusion.
- 일반주제명
- Molecular biology
- 일반주제명
- Biochemistry
- 일반주제명
- Systematic biology
- 기타저자
- Princeton University Molecular Biology
- 기본자료저록
- Dissertations Abstracts International. 85-10B.
- 전자적 위치 및 접속
- 로그인 후 원문을 볼 수 있습니다.
MARC
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■00520250211150930
■006m o d
■007cr#unu||||||||
■020 ▼a9798382193038
■035 ▼a(MiAaPQ)AAI30990201
■040 ▼aMiAaPQ▼cMiAaPQ
■0820 ▼a574
■1001 ▼aDAmico, Kevin Anthony.
■24510▼aCooperative Functions of the Retrograde Vesicle Fusion Machinery
■260 ▼a[Sl]▼bPrinceton University▼c2024
■260 1▼aAnn Arbor▼bProQuest Dissertations & Theses▼c2024
■300 ▼a109 p
■500 ▼aSource: Dissertations Abstracts International, Volume: 85-10, Section: B.
■500 ▼aIncludes supplementary digital materials.
■500 ▼aAdvisor: Hughson, Frederick M.
■5021 ▼aThesis (Ph.D.)--Princeton University, 2024.
■520 ▼aN-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs) mediate most intracellular membrane fusion events. SNAREs from apposed membranes interact to form membrane-bridging complexes that pull the membranes together, leading to lipid mixing and fusion. While SNAREs alone can drive membrane fusion, they are insufficient to fuse membranes at physiologically relevant speeds. To accelerate the process, membrane tethering complexes (MTC) mediate an initial attachment between a vesicle and a target membrane, and Sec1/Munc18 (SM) proteins accelerate the SNARE assembly step. How these families of proteins cooperate in vesicle capture and fusion, however, is poorly understood. Here, we present two structures of the Golgi-endoplasmic reticulum (ER) retrograde pathway fusion machinery. The first structure, the Saccharomyces cerevisiae Dsl1 MTC bound to the ER SNAREs Sec20 and Use1, is the first reported structure of a tethering complex engaged with other fusion machinery. Together, the trimeric Dsl1 complex and SNAREs form a rigid heteropentamer, the assembly of which is essential for yeast viability. This complex also bears unexpected similarities to the much-larger MTC exocyst, suggesting possible principles of MTC function. The second structure, the SM protein Sly1 bound to the ER SNARE Ufe1, constitutes the remainder of the ER-associated fusion machinery. The remaining Golgi-ER SNARE, Sec22, is embedded in and contributed by the Golgi-derived vesicle. Both the Dsl1 complex and Sly1 remain stably associated with SNAREs during SNARE assembly, resulting in an octameric supercomplex. Our data support a model in which the Dsl1 complex and Sly1 collaborate to localize SNAREs at the site of fusion and drive SNARE assembly and membrane fusion.
■590 ▼aSchool code: 0181.
■650 4▼aMolecular biology
■650 4▼aBiochemistry
■650 4▼aSystematic biology
■653 ▼aMembrane tethering complexes
■653 ▼aGolgi-endoplasmic reticulum
■653 ▼aTrafficking pathways
■653 ▼aSaccharomyces cerevisiae
■690 ▼a0307
■690 ▼a0487
■690 ▼a0423
■71020▼aPrinceton University▼bMolecular Biology.
■7730 ▼tDissertations Abstracts International▼g85-10B.
■790 ▼a0181
■791 ▼aPh.D.
■792 ▼a2024
■793 ▼aEnglish
■85640▼uhttp://www.riss.kr/pdu/ddodLink.do?id=T17160193▼nKERIS▼z이 자료의 원문은 한국교육학술정보원에서 제공합니다.
