Year: 2010
Type: dissertation
Abstract: Paknoosh PakarianCytokinesis describes the division of cytoplasm to produce two daughter cells, due to the formation and ingression of an actin-myosin contractile ring.The position and assembly of the contractile ring is directed by the central spindle during anaphase.The RhoGEF Ect2 localizes to the central spindle in a Cyk-4(MgcRacGAP)-dependent manner where it activates the GTPase RhoA to form the contractile ring in the central plane of the cell.Anillin is a conserved protein that contains N-terminal actin and myosin binding domains as well as a C-terminal AHD (Anillin Homology Domain) region that binds to RhoA, Ect2 and Cyk4 and a PH (Pleckstrin Homology) domain that interacts with Septins (another cytoskeletal component) and membrane phospholipids.Anillin plays a crucial role in the localization of active RhoA and is an early marker for the location of the contractile ring in many different eukaryotic cells.Anillin's interaction with RhoA, contractile ring components, the central spindle and the overlaying membrane, suggest that Anillin is a global regulator of cytokinesis.Although many of the core cytokinesis proteins have been identified, additional proteins likely regulate cytokinesis but have not been identified due to redundancy, or because they are also required for other cellular processes.To identify potential interactors of Anillin, and possibly of cytokinesis, a mass-spectrometry approach was used.A bacterially expressed Cterminal fragment of Anillin was used to pull down proteins from anaphase-synchronized cell lysates.The co-purified proteins were identified as GTPase regulators, cytoskeletal, mitotic, xi
Author: Paknoosh Pakarian
Language: English
Subfield: Cell Biology
Domain: Life Sciences
Open Access status: green
OpenAlex ID: W2164302161