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Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
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Structure and Function of p97 and Pex1/6 Type II AAA+ Complexes.

Paul Saffert1, Cordula Enenkel2, Petra Wendler1

  • 1Department of Biochemistry, Institute of Biochemistry and Biology, University of PotsdamPotsdam, Germany.

Frontiers in Molecular Biosciences
|June 15, 2017
PubMed
Summary
This summary is machine-generated.

Type II AAA+ protein complexes remodel substrates. This review details the structures and functions of p97/VCP and Pex1/Pex6, highlighting their roles in protein degradation and peroxisomal import.

Keywords:
Pex1Pex6cryo electron microscopyp97type II AAA+ ATPases

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Cell Biology

Background:

  • Type II AAA+ protein complexes are hexamers with two ATPase domains, crucial for diverse cellular activities.
  • Prominent examples include NSF, p97/VCP, Pex1/Pex6, Hsp104, and ClpB, involved in protein remodeling.
  • Understanding their conformational dynamics is key, but a uniform mechanism remains elusive.

Purpose of the Study:

  • To review the biochemical and cellular functions of p97/VCP and Pex1/Pex6 complexes.
  • To analyze and compare the structural information of these two Type II AAA+ complexes.
  • To emphasize recent electron microscopy findings and structural differences.

Main Methods:

  • Literature review of existing knowledge on p97/VCP and Pex1/Pex6.
  • Analysis of biochemical and cellular activities.
  • Focus on recent electron microscopy (EM) structural data.

Main Results:

  • p97/VCP and Pex1/Pex6 structurally remodel ubiquitinated proteins.
  • p97/VCP is involved in ER-associated protein degradation.
  • Pex1/Pex6 recycles Pex5 from the peroxisomal membrane during protein import.

Conclusions:

  • Type II AAA+ complexes exhibit diverse functions despite shared structural motifs.
  • Structural insights from EM reveal differences between p97/VCP and Pex1/Pex6.
  • Further research is needed to fully elucidate the uniform and distinct mechanisms of these complexes.