Scripps VIVO scripps research logo

  • Index
  • Log in
  • Home
  • People
  • Organizations
  • Research
  • Events
Search form
As of April 1st VIVO Scientific Profiles will no longer updated for faculty, and the link to VIVO will be removed from the library website. Faculty profile pages will continue to be updated via Interfolio. VIVO will continue being used behind the scenes to update graduate student profiles. Please contact helplib@scripps.edu if you have questions.
How to download citations from VIVO | Alternative profile options

Identification of a conserved F-box protein 6 interactor essential for endocytosis and cytokinesis in fission yeast

Academic Article
uri icon
  • Overview
  • Research
  • Identity
  • Additional Document Info
  • View All
scroll to property group menus

Overview

authors

  • Jourdain, I.
  • Spielewoy, N.
  • Thompson, J.
  • Dhut, S.
  • Yates III, John
  • Toda, T.

publication date

  • June 2009

journal

  • Biochemical Journal  Journal

abstract

  • The F-box domain is a degenerated motif consisting of approximately 40 amino acid residues that specifically bind Skp1, a core component of the SCF (Skp1-Cdc53/Cullin 1-F-box protein) ubiquitin ligase. Recent work, mainly performed in budding yeast, indicates that certain F-box proteins form non-SCF complexes together with Skp1 in the absence of cullins and play various roles in cell cycle and signalling pathways. However, it is not established whether these non-SCF complexes are unique to budding yeast or common in other eukaryotes. In the present paper, using TAP (tandem affinity purification) coupled to MudPIT (Multidimensional Protein Identification Technology) analysis, we have identified a novel conserved protein, Sip1, in fission yeast, as an interacting partner of an essential F-box protein Pof6. Sip1 is a large HEAT (huntingtin, elongation factor 3, the PR65/A subunit of protein phosphatase 2A and the lipid kinase Tor)-repeats containing protein (217 kDa) and forms a complex with Pof6 and Skp1. This complex does not contain cullins, indicating that it is a novel non-SCF complex. Like Pof6 and Skp1, Sip1 is essential for cell viability and temperature-sensitive sip1 mutants display cell division arrest as binucleate cells with septa. Sip1 localizes to the nucleus and dynamic cytoplasmic dots, which are shown in the present study to be endocytic vesicles. Consistent with this, sip1 mutants are defective in endocytosis. Furthermore, towards the end of cytokinesis, constriction of the actomyosin ring and dissociation of type II myosin and septum materials are substantially delayed in the absence of functional Sip1. These results indicate that the conserved Sip1 protein comprises a novel non-SCF F-box complex that plays an essential role in endocytosis, cytokinesis and cell division.

subject areas

  • Alleles
  • Cell Nucleus
  • Cytokinesis
  • Endocytosis
  • F-Box Proteins
  • Fungal Proteins
  • Genes, Essential
  • Genotype
  • Green Fluorescent Proteins
  • Immunoprecipitation
  • Microscopy, Fluorescence
  • Mutation
  • Protein Binding
  • Recombinant Fusion Proteins
  • Schizosaccharomyces
  • Schizosaccharomyces pombe Proteins
  • Temperature
scroll to property group menus

Research

keywords

  • F-box
  • HEAT repeats
  • MudPIT
  • cytokinesis
  • endocytosis
  • fission yeast
scroll to property group menus

Identity

PubMed Central ID

  • PMC2950653

International Standard Serial Number (ISSN)

  • 0264-6021

Digital Object Identifier (DOI)

  • 10.1042/bj20081659

PubMed ID

  • 19243310
scroll to property group menus

Additional Document Info

start page

  • 169

end page

  • 177

volume

  • 420

©2022 The Scripps Research Institute | Terms of Use | Powered by VIVO

  • About
  • Contact Us
  • Support