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You searched for +publisher:"Rutgers University" +contributor:("Carr, Chavela "). Showing records 1 – 3 of 3 total matches.

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Rutgers University

1. Pant, Saumya, 1979-. Membrane remodeling by novel regulators of the recycling endosome: the RME-1 and AMPH-1 partnership.

Degree: PhD, Cell and Developmental Biology, 2010, Rutgers University

Endocytic recycling is the process where by molecules traffic from endosomes back to the plasma membrane. This process is crucial for the maintenance of cellular homeostasis and cell polarity. C. elegans RME-1 and its mammalian homolog mRme-1/EHD1 are required for exit of cargo from the recycling endosome. The mechanism by which they control cargo exit has led to a proposal that they may function in formation of carrier tubules that break off from the recycling endosome. Recent studies suggested parallels of EHD family to the Dynamin GTPase superfamily of mechanoenzymes which function in membrane fission at the clathrin coated pit. Through a bioinformatics based screen we identified an interaction between RME-1 and AMPH-1, the only C. elegans member of Amphiphysin/BIN1 family of BAR-domain proteins. In mammalian neuronal synapses, Amphiphysin family proteins regulate the recruitment and activity of Dynamin for formation of vesicles. We established that AMPH-1 co localizes with RME-1 on recycling endosomes in vivo, amph-1 deletion mutants are defective in recycling endosome morphology and function and that AMPH-1 and RME-1 cooperatively promote the recycling of transmembrane cargo. in vitro we found that purified recombinant AMPH-1/RME-1 co-assemble on membranes to produce short, coated tubules which are qualitatively distinct from those produced by either protein alone. We have established that AMPH-1 and RME-1 serve as a novel membrane tubulation and possibly fission machinery at the recycling endosome, an interaction that is conserved in mammals. We also investigated the function of a serine/threonine kinase of the germinal center kinase family (GCK-2) which is known to bind two Rabs, RAB-10 and RAB-8, which function in endocytic recycling. We established that GCK-2 is a novel effector of RAB-8 in regulating RME-1 labeled recycling endosomes. In select functions, it may serve as a RAB-10 effector. This may be an example of RABs being sequentially activated by binding the same effector. This study identifies a novel function for a germinal center kinase proteins whose only known function relates to the MAPK signaling cascade. We recently established an interaction between GCK-2 and AMPH-1. We hypothesize that this interaction could serve as a hub which ties together the major recycling endosome interactions mapped for RME-1/AMPH-1 as well as with RAB-8/RAB-10.

Advisors/Committee Members: Pant, Saumya, 1979- (author), Rongo, Christopher (chair), Grant, Barth (internal member), Driscoll, Monica (internal member), Matsumura, Fumio (internal member), Carr, Chavela (outside member).

Subjects/Keywords: Cell membranes; Endosomes

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6th Edition):

Pant, Saumya, 1. (2010). Membrane remodeling by novel regulators of the recycling endosome: the RME-1 and AMPH-1 partnership. (Doctoral Dissertation). Rutgers University. Retrieved from http://hdl.rutgers.edu/1782.2/rucore10001600001.ETD.000052268

Chicago Manual of Style (16th Edition):

Pant, Saumya, 1979-. “Membrane remodeling by novel regulators of the recycling endosome: the RME-1 and AMPH-1 partnership.” 2010. Doctoral Dissertation, Rutgers University. Accessed November 14, 2019. http://hdl.rutgers.edu/1782.2/rucore10001600001.ETD.000052268.

MLA Handbook (7th Edition):

Pant, Saumya, 1979-. “Membrane remodeling by novel regulators of the recycling endosome: the RME-1 and AMPH-1 partnership.” 2010. Web. 14 Nov 2019.

Vancouver:

Pant, Saumya 1. Membrane remodeling by novel regulators of the recycling endosome: the RME-1 and AMPH-1 partnership. [Internet] [Doctoral dissertation]. Rutgers University; 2010. [cited 2019 Nov 14]. Available from: http://hdl.rutgers.edu/1782.2/rucore10001600001.ETD.000052268.

Council of Science Editors:

Pant, Saumya 1. Membrane remodeling by novel regulators of the recycling endosome: the RME-1 and AMPH-1 partnership. [Doctoral Dissertation]. Rutgers University; 2010. Available from: http://hdl.rutgers.edu/1782.2/rucore10001600001.ETD.000052268

2. Harrison, David A., 1965-. Identification and characterization of critical laminin-111 sequences required for polymerization and cell surface anchorage and the requirement of both activities for proper basement membrane formation and other events.

Degree: Biochemistry, 2012, Rutgers University

Subjects/Keywords: Proteins – Affinity labeling; Polymerization

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6th Edition):

Harrison, David A., 1. (2012). Identification and characterization of critical laminin-111 sequences required for polymerization and cell surface anchorage and the requirement of both activities for proper basement membrane formation and other events. (Thesis). Rutgers University. Retrieved from http://hdl.rutgers.edu/1782.1/rucore10001600001.ETD.000065159

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16th Edition):

Harrison, David A., 1965-. “Identification and characterization of critical laminin-111 sequences required for polymerization and cell surface anchorage and the requirement of both activities for proper basement membrane formation and other events.” 2012. Thesis, Rutgers University. Accessed November 14, 2019. http://hdl.rutgers.edu/1782.1/rucore10001600001.ETD.000065159.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7th Edition):

Harrison, David A., 1965-. “Identification and characterization of critical laminin-111 sequences required for polymerization and cell surface anchorage and the requirement of both activities for proper basement membrane formation and other events.” 2012. Web. 14 Nov 2019.

Vancouver:

Harrison, David A. 1. Identification and characterization of critical laminin-111 sequences required for polymerization and cell surface anchorage and the requirement of both activities for proper basement membrane formation and other events. [Internet] [Thesis]. Rutgers University; 2012. [cited 2019 Nov 14]. Available from: http://hdl.rutgers.edu/1782.1/rucore10001600001.ETD.000065159.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Harrison, David A. 1. Identification and characterization of critical laminin-111 sequences required for polymerization and cell surface anchorage and the requirement of both activities for proper basement membrane formation and other events. [Thesis]. Rutgers University; 2012. Available from: http://hdl.rutgers.edu/1782.1/rucore10001600001.ETD.000065159

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation


Rutgers University

3. Hashizume, Kristina Kaori. Probing the universal role of Sec1/Munc18 proteins by mutagenesis of yeast Sec1.

Degree: MS, Microbiology and Molecular Genetics, 2008, Rutgers University

The Sec1/Munc18 (SM) family of proteins is essential for intracellular vesicle trafficking in eukaryotic cells. Sec1, the SM protein at the yeast plasma membrane, is required for membrane fusion leading to secretion and cell growth. Fusion of exocytic vesicles targeted to the plasma membrane occurs in two stages. The vesicle is first tethered to the membrane by a protein complex called the exocyst. Essential membrane-associated proteins known as the soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs) located on both the plasma membrane and the vesicle assemble together to form a stable four-helix bundle called the SNARE complex. In the second step, Sec1 binds to the assembled SNARE complex and there is fusion of the two membranes. Sec1 has been shown to bind the SNARE complex, but the exact role and mechanism of Sec1 function remains unknown. In this study, site-directed mutagenesis was used to investigate the significance of highly conserved salt bridges in SM proteins and define the SNARE complex binding surface on Sec1 with data from random mutants studied by Yi-Shan Cheng and Jenna Hutton. In addition, Sec1 mutants with a novel phenotype were generated that may support a role for Sec1 in vesicle tethering. Advisors/Committee Members: Hashizume, Kristina Kaori (author), Grant, Barth (chair), Kinzy, Terri (internal member), Carr, Chavela (internal member).

Subjects/Keywords: Membrane proteins; Mutagenesis; Yeast fungi

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6th Edition):

Hashizume, K. K. (2008). Probing the universal role of Sec1/Munc18 proteins by mutagenesis of yeast Sec1. (Masters Thesis). Rutgers University. Retrieved from http://hdl.rutgers.edu/1782.2/rucore10001600001.ETD.17323

Chicago Manual of Style (16th Edition):

Hashizume, Kristina Kaori. “Probing the universal role of Sec1/Munc18 proteins by mutagenesis of yeast Sec1.” 2008. Masters Thesis, Rutgers University. Accessed November 14, 2019. http://hdl.rutgers.edu/1782.2/rucore10001600001.ETD.17323.

MLA Handbook (7th Edition):

Hashizume, Kristina Kaori. “Probing the universal role of Sec1/Munc18 proteins by mutagenesis of yeast Sec1.” 2008. Web. 14 Nov 2019.

Vancouver:

Hashizume KK. Probing the universal role of Sec1/Munc18 proteins by mutagenesis of yeast Sec1. [Internet] [Masters thesis]. Rutgers University; 2008. [cited 2019 Nov 14]. Available from: http://hdl.rutgers.edu/1782.2/rucore10001600001.ETD.17323.

Council of Science Editors:

Hashizume KK. Probing the universal role of Sec1/Munc18 proteins by mutagenesis of yeast Sec1. [Masters Thesis]. Rutgers University; 2008. Available from: http://hdl.rutgers.edu/1782.2/rucore10001600001.ETD.17323

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