The Cdc48/p97-Ufd1-Npl4 Complex: Its Potential Role in Coordinating Cellular Morphogenesis During the M-G1 Transition

Cell Cycle. 2004 Apr;3(4):422-4. Epub 2004 Apr 1.

Abstract

The AAA ATPase Cdc48/p97 together with its adaptors, Ufd1-Npl4, regulate membrane-related functions and mitotic spindle disassembly by directly binding to membrane-associated proteins or spindle assembly factors, modulating their interactions with membranes or spindles, respectively. Here, we discuss the possibility that the Cdc48/ p97-Ufd1-Npl4 complex has a more general role in mediating morphological transitions as the cell exits mitosis and enters G(1).

MeSH terms

  • Adenosine Triphosphatases
  • Animals
  • Antigens, Neoplasm
  • Cell Cycle Proteins / metabolism*
  • Cell Nucleus / metabolism
  • G1 Phase
  • Gene Expression Regulation
  • Melanoma-Specific Antigens
  • Mitosis
  • Neoplasm Proteins / metabolism*
  • Nuclear Pore Complex Proteins / metabolism*
  • Nucleocytoplasmic Transport Proteins
  • Phosphorylation
  • Protein Binding
  • Saccharomyces cerevisiae / metabolism
  • Saccharomyces cerevisiae Proteins / metabolism*
  • Ubiquitin / metabolism
  • Valosin Containing Protein
  • Vesicular Transport Proteins
  • Xenopus

Substances

  • Antigens, Neoplasm
  • Cell Cycle Proteins
  • Melanoma-Specific Antigens
  • NPL4 protein, S cerevisiae
  • Neoplasm Proteins
  • Nuclear Pore Complex Proteins
  • Nucleocytoplasmic Transport Proteins
  • Saccharomyces cerevisiae Proteins
  • UFD1 protein, S cerevisiae
  • Ubiquitin
  • Vesicular Transport Proteins
  • Adenosine Triphosphatases
  • CDC48 protein, S cerevisiae
  • Valosin Containing Protein