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Discovering how inner nuclear membra...

Johnson, Isabel Emily.

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Discovering how inner nuclear membrane protein, LEM2, orchestrates timely nuclear envelope reformation during open mitosis.

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	Discovering how inner nuclear membrane protein, LEM2, orchestrates timely nuclear envelope reformation during open mitosis./
作者:	Johnson, Isabel Emily.
出版者:	Ann Arbor : ProQuest Dissertations & Theses, : 2020,
面頁冊數:	70 p.
附註:	Source: Dissertations Abstracts International, Volume: 81-10, Section: B.
Contained By:	Dissertations Abstracts International81-10B.
標題:	Biochemistry. -
電子資源:	https://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=27741998
ISBN:	9781658492898

Discovering how inner nuclear membrane protein, LEM2, orchestrates timely nuclear envelope reformation during open mitosis.
Johnson, Isabel Emily.

Discovering how inner nuclear membrane protein, LEM2, orchestrates timely nuclear envelope reformation during open mitosis. - Ann Arbor : ProQuest Dissertations & Theses, 2020 - 70 p.

Source: Dissertations Abstracts International, Volume: 81-10, Section: B.

Thesis (Ph.D.)--University of California, San Francisco, 2020.

.

Membranes are fundamental to cellular life. They define the cellular border and establish biochemically specialized subcellular compartments. As cell grow, change, and divide, cellular membranes are remodeled accordingly: undergoing membrane fission and fusion to maintain cellular architecture. For example, the nuclear membrane that organizes and protects DNA is remodeled during cell division. In cells that undergo "open mitosis", the nuclear membrane is fully disassembled to allow chromosomes to be segregated by the spindle apparatus and reassembled following chromosome segregation. Understanding how cells remodel nuclear membranes to rebuild nuclei with every cell division is critical to understanding the core principals of membrane biology that underlie cellular life. In my dissertation, I describe how a membrane fusion complex is organized to seal holes in the reforming nuclear envelope that are occupied by spindle microtubules. Using biochemical approaches, I find that an inner nuclear membrane protein, called LEM2, uses multivalent, low-affinity binding interactions to condense in a liquid-like phase at the junction of the nuclear envelope, chromatin, and residual spindle microtubules. There, LEM2 activates the ESCRT protein, CHMP7, in a looping copolymer. Together, the fluid LEM2 toroid and structured LEM2-CHMP7 copolymer collaborate to serve as a molecular "O-ring" for early nuclear sealing. Furthermore, the LEM2-CHMP7 ring serves as a foundation for the membrane-remodeling ESCRT-III complex to execute coupled spindle disassembly and membrane fusion. This work establishes a new paradigm in membrane organization, in which a liquid-like protein phase can function as both a barrier within a discontinuous membrane and a scaffold for membrane fusion factors.

ISBN: 9781658492898Subjects--Topical Terms:

518028
Biochemistry.
Subjects--Index Terms:

CHMP7

Discovering how inner nuclear membrane protein, LEM2, orchestrates timely nuclear envelope reformation during open mitosis.
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020 $a 9781658492898
035 $a (MiAaPQ)AAI27741998
035 $a AAI27741998
040 $a MiAaPQ $c MiAaPQ
100 1 $a Johnson, Isabel Emily. $0 (orcid)0000-0002-3294-4423 $3 3769832
245 1 0 $a Discovering how inner nuclear membrane protein, LEM2, orchestrates timely nuclear envelope reformation during open mitosis.
260 1 $a Ann Arbor : $b ProQuest Dissertations & Theses, $c 2020
300 $a 70 p.
500 $a Source: Dissertations Abstracts International, Volume: 81-10, Section: B.
500 $a Advisor: Frost, Adam.
502 $a Thesis (Ph.D.)--University of California, San Francisco, 2020.
506 $a .
520 $a Membranes are fundamental to cellular life. They define the cellular border and establish biochemically specialized subcellular compartments. As cell grow, change, and divide, cellular membranes are remodeled accordingly: undergoing membrane fission and fusion to maintain cellular architecture. For example, the nuclear membrane that organizes and protects DNA is remodeled during cell division. In cells that undergo "open mitosis", the nuclear membrane is fully disassembled to allow chromosomes to be segregated by the spindle apparatus and reassembled following chromosome segregation. Understanding how cells remodel nuclear membranes to rebuild nuclei with every cell division is critical to understanding the core principals of membrane biology that underlie cellular life. In my dissertation, I describe how a membrane fusion complex is organized to seal holes in the reforming nuclear envelope that are occupied by spindle microtubules. Using biochemical approaches, I find that an inner nuclear membrane protein, called LEM2, uses multivalent, low-affinity binding interactions to condense in a liquid-like phase at the junction of the nuclear envelope, chromatin, and residual spindle microtubules. There, LEM2 activates the ESCRT protein, CHMP7, in a looping copolymer. Together, the fluid LEM2 toroid and structured LEM2-CHMP7 copolymer collaborate to serve as a molecular "O-ring" for early nuclear sealing. Furthermore, the LEM2-CHMP7 ring serves as a foundation for the membrane-remodeling ESCRT-III complex to execute coupled spindle disassembly and membrane fusion. This work establishes a new paradigm in membrane organization, in which a liquid-like protein phase can function as both a barrier within a discontinuous membrane and a scaffold for membrane fusion factors.
590 $a School code: 0034.
650 4 $a Biochemistry. $3 518028
650 4 $a Cellular biology. $3 3172791
653 $a CHMP7
653 $a ESCRT-III
653 $a LEM2
653 $a Mitosis
653 $a Nuclear reformation
653 $a Phase separation
690 $a 0487
690 $a 0379
710 2 $a University of California, San Francisco. $b Biochemistry and Molecular Biology. $3 1263088
773 0 $t Dissertations Abstracts International $g 81-10B.
790 $a 0034
791 $a Ph.D.
792 $a 2020
793 $a English
856 4 0 $u https://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=27741998