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Regulation of Nuclear Envelope Remod...

Shankar, Raakhee.

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Regulation of Nuclear Envelope Remodeling by the ESCRT Machinery.

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	Regulation of Nuclear Envelope Remodeling by the ESCRT Machinery./
作者:	Shankar, Raakhee.
出版者:	Ann Arbor : ProQuest Dissertations & Theses, : 2021,
面頁冊數:	250 p.
附註:	Source: Dissertations Abstracts International, Volume: 83-03, Section: B.
Contained By:	Dissertations Abstracts International83-03B.
標題:	Cellular biology. -
電子資源:	https://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=28719965
ISBN:	9798538120857

Regulation of Nuclear Envelope Remodeling by the ESCRT Machinery.
Shankar, Raakhee.

Regulation of Nuclear Envelope Remodeling by the ESCRT Machinery. - Ann Arbor : ProQuest Dissertations & Theses, 2021 - 250 p.

Source: Dissertations Abstracts International, Volume: 83-03, Section: B.

Thesis (Ph.D.)--The University of Wisconsin - Madison, 2021.

.

The endosomal sorting complex required for transport (ESCRT) machinery participates in a wide range of cellular processes. These processes include multivesicular endosome biogenesis, nuclear envelope reformation and repair, cytokinesis, plasma membrane repair, among others. The common thread between these diverse cellular processes is that the ESCRT machinery remodels membranes displaying similar topology. In the work presented in this thesis, I focus on elucidating the mechanisms by which the ESCRT machinery maintains the nuclear envelope (NE) integrity.The eukaryotic NE encloses the genome and forms a barrier allowing selective transport of material between the nucleus and the cytoplasm. This barrier is disrupted when the cell undergoes open mitosis. It is therefore necessary to reform the NE on mitotic exit. The ESCRT machinery has been implicated in remodeling the NE after mitosis to reestablish nuclear compartmentalization. Additional studies suggest that in migrating cells, interphase NE undergoes transient ruptures. Rapid membrane remodeling is required in such cases to maintain genome integrity. Failure to restore the nuclear barrier function may result in DNA damage.In this work I utilize the stereotypic first mitotic division of the C. elegans embryo to investigate the quality control mechanisms present during NE reformation. Work presented in both Chapters 2 and 3 are studies done in a developing organism. Collaborative work presented in Chapter 2 reveals a role for CNEP-1 which regulates synthesis of glycerolipids, and in conjunction with the ESCRT-III machinery limits ER sheet incorporation at NE ruptures following lamin depletion. In Chapter 3 I investigate the role of CHMP7, an adaptor for the ESCRT machinery at the NE, in regulating the ESCRT-III machinery at the reforming NE after mitosis as well as under conditions with a compromised nuclear lamina. I show that in C. elegans, CHMP7 localizes to the inner nuclear membrane throughout interphase. This is striking because in yeast and mammalian cell lines, CHMP7 localizes to the ER and localizes at the reforming NE transiently during late anaphase. Using electron tomography, I demonstrate that impairment in ESCRT function leads to formation of NE invaginations originating from the inner nuclear membrane. These tubules are enriched with INM proteins including LEM2 (Ce MAN1), LMN1 (lamin), SUN1 (LINC complex) as well as every subunit of the ESCRT-III machinery except VPS20. I also identify the presence of intranuclear vesicles emanating from the INM tubules suggesting that the ESCRT machinery is involved in pruning these tubules to maintain INM integrity. Embryos lacking CHMP7 do not display defects in NE closure suggesting the presence of multiple redundant mechanisms to ensure NE closure. To that effect, I propose a role for VPS60/CHMP5 in maintaining the health of C. elegans gonad by regulating germline apoptosis.

ISBN: 9798538120857Subjects--Topical Terms:

3172791
Cellular biology.
Subjects--Index Terms:

C. elegans

Regulation of Nuclear Envelope Remodeling by the ESCRT Machinery.
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300 $a 250 p.
500 $a Source: Dissertations Abstracts International, Volume: 83-03, Section: B.
500 $a Advisor: Audhya, Anjon.
502 $a Thesis (Ph.D.)--The University of Wisconsin - Madison, 2021.
506 $a .
520 $a The endosomal sorting complex required for transport (ESCRT) machinery participates in a wide range of cellular processes. These processes include multivesicular endosome biogenesis, nuclear envelope reformation and repair, cytokinesis, plasma membrane repair, among others. The common thread between these diverse cellular processes is that the ESCRT machinery remodels membranes displaying similar topology. In the work presented in this thesis, I focus on elucidating the mechanisms by which the ESCRT machinery maintains the nuclear envelope (NE) integrity.The eukaryotic NE encloses the genome and forms a barrier allowing selective transport of material between the nucleus and the cytoplasm. This barrier is disrupted when the cell undergoes open mitosis. It is therefore necessary to reform the NE on mitotic exit. The ESCRT machinery has been implicated in remodeling the NE after mitosis to reestablish nuclear compartmentalization. Additional studies suggest that in migrating cells, interphase NE undergoes transient ruptures. Rapid membrane remodeling is required in such cases to maintain genome integrity. Failure to restore the nuclear barrier function may result in DNA damage.In this work I utilize the stereotypic first mitotic division of the C. elegans embryo to investigate the quality control mechanisms present during NE reformation. Work presented in both Chapters 2 and 3 are studies done in a developing organism. Collaborative work presented in Chapter 2 reveals a role for CNEP-1 which regulates synthesis of glycerolipids, and in conjunction with the ESCRT-III machinery limits ER sheet incorporation at NE ruptures following lamin depletion. In Chapter 3 I investigate the role of CHMP7, an adaptor for the ESCRT machinery at the NE, in regulating the ESCRT-III machinery at the reforming NE after mitosis as well as under conditions with a compromised nuclear lamina. I show that in C. elegans, CHMP7 localizes to the inner nuclear membrane throughout interphase. This is striking because in yeast and mammalian cell lines, CHMP7 localizes to the ER and localizes at the reforming NE transiently during late anaphase. Using electron tomography, I demonstrate that impairment in ESCRT function leads to formation of NE invaginations originating from the inner nuclear membrane. These tubules are enriched with INM proteins including LEM2 (Ce MAN1), LMN1 (lamin), SUN1 (LINC complex) as well as every subunit of the ESCRT-III machinery except VPS20. I also identify the presence of intranuclear vesicles emanating from the INM tubules suggesting that the ESCRT machinery is involved in pruning these tubules to maintain INM integrity. Embryos lacking CHMP7 do not display defects in NE closure suggesting the presence of multiple redundant mechanisms to ensure NE closure. To that effect, I propose a role for VPS60/CHMP5 in maintaining the health of C. elegans gonad by regulating germline apoptosis.
590 $a School code: 0262.
650 4 $a Cellular biology. $3 3172791
650 4 $a Molecular biology. $3 517296
650 4 $a DNA methylation. $3 3560639
650 4 $a Cancer. $3 634186
650 4 $a Cytoplasm. $3 3337992
650 4 $a Cytoskeleton. $3 549552
650 4 $a Biosynthesis. $3 516407
650 4 $a Mutation. $3 837917
650 4 $a Polymerization. $3 560492
650 4 $a Genomes. $3 592593
650 4 $a Breakdowns. $3 3682712
650 4 $a Lipids. $3 558980
650 4 $a Apoptosis. $3 600650
650 4 $a Kinases. $3 3558077
650 4 $a Cell cycle. $3 766119
650 4 $a Proteins. $3 558769
650 4 $a Membranes. $3 1531702
650 4 $a Human immunodeficiency virus--HIV. $3 3564909
650 4 $a Permeability. $3 915594
650 4 $a Cyclin-dependent kinases. $3 868634
650 4 $a Chromosomes. $3 638948
650 4 $a Worms. $3 3561322
650 4 $a Phosphorylation. $3 816803
650 4 $a Deformation. $2 lcstt $3 3267001
650 4 $a Enzymes. $3 520899
653 $a C. elegans
653 $a chmp7
653 $a ESCRT
653 $a Inner nuclear membrane
653 $a Nuclear envelope
690 $a 0379
690 $a 0307
710 2 $a The University of Wisconsin - Madison. $b Biomolecular Chemistry. $3 3769848
773 0 $t Dissertations Abstracts International $g 83-03B.
790 $a 0262
791 $a Ph.D.
792 $a 2021
793 $a English
856 4 0 $u https://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=28719965