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oai:www.ideals.illinois.edu:2142/86665 2023-07-11 col_2142_5131 col_2142_16338 com_2142_5130 com_2142_16337 com_2142_14793 com_2142_8903

Vladimir I. Gelfand Roland, Joseph Thomas Edward 2015-09-28T15:17:16Z 2015-09-28T15:17:16Z 10000-01-01 2004 2004 Myosin V is required for the proper transport and localization of specific organelles along actin filaments in many cell types. Two independent kinases, Calcium/calmodulin-dependent kinase II (CaMKII) and p21-activated kinase-1 (PAK1), are able to phosphorylate the globular tail of myosin V. Mutation analysis and mass spectrometry were used to determine the actual site of phosphorylation for each kinase. The target of CaMKII phosphorylation is the serine residue at position 1650 in the globular tail of mouse myosin Va, while PAK1 phosphorylates the serine residue located at position 1649. The tandem localization of these two, independent phosphorylation sites suggests that this region of the protein is central to motor regulation. During mitosis, CaMKII phosphorylation of myosin V inhibits the ability of the motor to bind to Xenopus melanosomes. Similarly, myosin V recruitment to mouse phagosomes during phagocytosis is blocked by PAK1 phosphorylation. Thus, the binding of myosin V to cargo is regulated by phosphorylation of the tail domain, and may represent a common mechanism of regulation of vertebrate myosin V. Made available in DSpace on 2015-09-28T15:17:16Z (GMT). No. of bitstreams: 2 license.txt: 4848 bytes, checksum: 96035ab3f5e1c23cc7138a224ce498bd (MD5) 3131017.pdf: 4159526 bytes, checksum: 5b409ac76c17dafef54112b65ea02161 (MD5) Previous issue date: 2004 Embargo set by: Seth Robbins for item 87946 Lift date: Forever Reason: Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs U of I Only 82 p. Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 2004. http://hdl.handle.net/2142/86665 (MiAaPQ)AAI3131017 eng Biology, Cell Regulation of Myosin V-Cargo Interactions by Phosphorylation text Microbiology Microbiology University of Illinois at Urbana-Champaign Dissertation Ph.D.