Abstract
Spatiotemporal organisation of eukaryotic cells is established and maintained by the cytoskeleton, a highly dynamic and complex network of structural and signalling proteins. Many components of the cytoskeleton are functionally and structurally conserved between humans and yeast. Among these are verprolin (Vrp1p) in yeast and its human ortholog Wiskott-Aldrich syndrome protein (WASP)-interacting protein (WIP). Much of our understanding of the function of these proteins has come from genetic analysis in yeast. Verprolin-deficient yeast cells exhibit defects in cytokinesis, endocytosis, and actin cytoskeleton polarisation. Verprolin binds actin, the yeast ortholog of human WASP (Las17p or Bee1p), and the yeast ortholog of human PSTPIP1 (Hof1p or Cyk2p). We propose that verprolin acts as a chaperone that by transient bimolecular interactions maintains the proper function of its partners. Verprolin-related proteins and partners are implicated in cancer, immunodeficiency, and neurodegeneration. Therefore, elucidating how verprolin functions will have major impacts in cell biology and medicine.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
