Studies of Alpha Kinase 1 and its potential to influence cytoskeletal reorganization
| العنوان: | Studies of Alpha Kinase 1 and its potential to influence cytoskeletal reorganization |
|---|---|
| المؤلفون: | Burgett, Kyle D. |
| بيانات النشر: | [Greensboro, N.C.] : [University of North Carolina at Greensboro], [2016] |
| تفاصيل مُضافة: | NC Digital Online Collection of Knowledge and Scholarship (NCDOCKS) |
| وصف مادي: | v, 55 pages : illustrations, digital, PDF file 2.61 MB. |
| Supplemental Data: | System requirements: PC, World Wide Web browser, PDF reader. Available online via NCDOCKS. Mode of access: World Wide Web. |
| مستخلص: | "Maintaining and remodeling the actin cytoskeleton is a critical part of normal cellular functioning for all eukaryotes, as it is crucial for cell movement, endocytosis, exocytosis, and maintaining cellular morphology. Within the social amoeba Dictyostelium discoideum, myosin II associates with the actin cytoskeleton and is directly responsible for the contraction of opposing actin filaments. Cytoskeletal remodeling is achieved by cycling myosin II between a bipolar filamentous form and a monomeric form. In Dictyostelium, the family of alpha kinases known as myosin heavy chain kinases (MHCKs) has been shown to be the primary regulators of myosin II bipolar filament turnover. By phosphorylating specific threonine residues on the tail region of the myosin II protein, MHCKs control the assembly/disassembly of myosin II filaments. Alpha Kinase 1 (AK1) represents a previously uncharacterized member of the MHCK family in Dictyostelium. The data presented in this thesis provides evidence that AK1 can influence myosin II bipolar filament turnover and indeed act as a myosin II heavy chain kinase. Overexpression of AK1 yields a myosin II null phenotype, characterized by cytoskeletal defects arising from elevated levels of phosphorylated monomeric myosin II, as evidenced by 1) an inability to complete cytokinesis in suspension culture, and 2) delayed multicellular development. Localization studies performed with GFP-tagged AK1 reveal a localization pattern that is consistent with a role for AK1 in vesicle trafficking, unique amongst the MHCKs. Taken together, these data support the hypothesis that AK1 can function as a MHCK in Dictyostelium and suggest that more detailed biochemical and cellular studies of AK1 are warranted to fully characterize this unique protein and its potential role in regulating myosin II activity."--Abstract from author supplied metadata. |
| الموضوعات: | Dictyostelium discoideum., Cytoskeleton., Myosin., Dictyostelium discoideum., Cytosquelette., Myosine., Cytoskeleton, Dictyostelium discoideum, Myosin |
| مصطلحات الفهرس: | dissertations., Academic theses, Academic theses., Thèses et écrits académiques. |
| URL: | |
| ملاحظة: | Title from PDF title page (viewed July 25, 2017). Directed by Paul Steimle ; submitted to the Dept. of Biology. Includes bibliographical references (pages 31-33). |
| أرقام أخرى: | NGU oai:libres.uncg.edu/19547 979987374 |
| المصدر المساهم: | From OAIster®, provided by the OCLC Cooperative. |
| رقم الأكسشن: | edsoai.ocn979987374 |
| قاعدة البيانات: | OAIster |
| الوصف غير متاح. |