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Dictyostelium Discoideum Protein Kin...

Singh, Sean.

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Dictyostelium Discoideum Protein Kinase C-Orthologue pkcA Regulates the Actin Cytoskeleton Through Interaction with Phospholipase D and p21-Activated Kinase.

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	Dictyostelium Discoideum Protein Kinase C-Orthologue pkcA Regulates the Actin Cytoskeleton Through Interaction with Phospholipase D and p21-Activated Kinase./
作者:	Singh, Sean.
出版者:	Ann Arbor : ProQuest Dissertations & Theses, : 2020,
面頁冊數:	113 p.
附註:	Source: Dissertations Abstracts International, Volume: 81-12, Section: B.
Contained By:	Dissertations Abstracts International81-12B.
標題:	Molecular biology. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=27961105
ISBN:	9798641335339

Dictyostelium Discoideum Protein Kinase C-Orthologue pkcA Regulates the Actin Cytoskeleton Through Interaction with Phospholipase D and p21-Activated Kinase.
Singh, Sean.

Dictyostelium Discoideum Protein Kinase C-Orthologue pkcA Regulates the Actin Cytoskeleton Through Interaction with Phospholipase D and p21-Activated Kinase. - Ann Arbor : ProQuest Dissertations & Theses, 2020 - 113 p.

Source: Dissertations Abstracts International, Volume: 81-12, Section: B.

Thesis (Ph.D.)--City University of New York, 2020.

This item must not be sold to any third party vendors.

Proper regulation of the actin cytoskeleton is crucial to many cellular processes. Many of these processes are regulated by extracellular signaling cues, which direct changes in the actin cytoskeleton, resulting in changes to cellular morphology, and directed motility. The social amoeba, Dictyostelium discoideum, is used as a simple model system to study the translation of extracellular signals to the actin cytoskeleton. When starved, these unicellular amoebae undergo a multicellular developmental process characterized by a tightly regulated sequence of signaling events. This results in chemotaxis and formation of a multicellular aggregate, and ultimately cell differentiation and the formation of a fruiting body. pkcA, a putative Protein Kinase C-orthologue, has previously been shown to regulate development and fruiting body formation. Here we show that pkcA is involved in cell density sensing, chemotactic signaling, cell morphology, and cell-cell cohesion. Additionally, we show through epistasis analysis, that pkcA regulates these processes through a functional interaction with pldB, a D. discoideum PLD-orthologue. Lastly, we provide evidence that pakD, a p21-activated kinase, acts between pkcA and pldB in the regulation of development. Given that both pldB and pakD have been shown to regulate the actin cytoskeleton during chemotaxis and development, this provides a mechanism for pkcA to influence the organization and assembly of the actin cytoskeleton.

ISBN: 9798641335339Subjects--Topical Terms:

517296
Molecular biology.
Subjects--Index Terms:

Actin cytoskeleton

Dictyostelium Discoideum Protein Kinase C-Orthologue pkcA Regulates the Actin Cytoskeleton Through Interaction with Phospholipase D and p21-Activated Kinase.
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520 $a Proper regulation of the actin cytoskeleton is crucial to many cellular processes. Many of these processes are regulated by extracellular signaling cues, which direct changes in the actin cytoskeleton, resulting in changes to cellular morphology, and directed motility. The social amoeba, Dictyostelium discoideum, is used as a simple model system to study the translation of extracellular signals to the actin cytoskeleton. When starved, these unicellular amoebae undergo a multicellular developmental process characterized by a tightly regulated sequence of signaling events. This results in chemotaxis and formation of a multicellular aggregate, and ultimately cell differentiation and the formation of a fruiting body. pkcA, a putative Protein Kinase C-orthologue, has previously been shown to regulate development and fruiting body formation. Here we show that pkcA is involved in cell density sensing, chemotactic signaling, cell morphology, and cell-cell cohesion. Additionally, we show through epistasis analysis, that pkcA regulates these processes through a functional interaction with pldB, a D. discoideum PLD-orthologue. Lastly, we provide evidence that pakD, a p21-activated kinase, acts between pkcA and pldB in the regulation of development. Given that both pldB and pakD have been shown to regulate the actin cytoskeleton during chemotaxis and development, this provides a mechanism for pkcA to influence the organization and assembly of the actin cytoskeleton.
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