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Related Experiment Videos

ARF- and coatomer-mediated peroxisomal vesiculation.

M Anton1, M Passreiter, D Lay

  • 1Biochemie-Zentrum, Universität Heidelberg, D-69120 Heidelberg, Germany.

Cell Biochemistry and Biophysics
|May 2, 2001
PubMed
Summary

Researchers identified Pex11-1p, a peroxisomal membrane protein involved in peroxisome biogenesis. Its dilysine motif mediates binding to ARF and coatomer, influencing peroxisome number and structure.

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Peroxisomes are vital organelles involved in various metabolic processes.
  • The biogenesis and regulation of peroxisome number and morphology are complex.
  • Integral peroxisomal membrane proteins play key roles in organelle dynamics.

Purpose of the Study:

  • To characterize the clofibrate-inducible 26-kDa integral peroxisomal membrane protein (Pex11-1p) from rat liver.
  • To identify homologous proteins and elucidate the molecular mechanisms of Pex11-1p function.
  • To investigate the role of Pex11-1p in peroxisome vesiculation and biogenesis.

Main Methods:

  • Molecular cloning and cDNA database screening to identify Pex11-1p and its homolog (Pex11-2p).
  • Topology studies using molecular biology techniques to determine membrane orientation.

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  • Biochemical assays with isolated peroxisomes, cytosol, and specific ligands (ATP, GTPγS) to study protein binding.
  • Expression studies in wild-type and mutant Chinese hamster ovary (CHO) cells to assess functional impact.

    • Main Results:

    • Pex11-1p possesses two transmembrane domains with N- and C-termini facing the cytoplasm.
    • The C-terminal dilysine motif (-KXKXX-COOH) of Pex11-1p mediates binding of ADP-ribosylation factor (ARF) and coatomer to peroxisomes.
    • Expression of Pex11-1p increased peroxisome number in wild-type CHO cells.
    • In coatomer-deficient CHO cells, Pex11-1p induced peroxisomal elongation and tubulation instead of proliferation.

    Conclusions:

    • Pex11-1p, through its dilysine motif, recruits ARF and coatomer to peroxisomes, mediating peroxisomal vesiculation.
    • The findings provide a molecular mechanism for ARF- and coatomer-dependent peroxisome dynamics.
    • Two models are proposed to integrate these findings into the broader context of peroxisome biogenesis.