Rat prominin, like its mouse and human orthologues, is a pentaspan membrane glycoprotein

D Corbeil1, C A Fargeas, W B Huttner

  • 1Max Planck Institute of Molecular Cell Biology and Genetics, Pfotenhauerstrasse 108, Dresden, D-01307, Germany.

Insights

Rat prominin is a full-length pentaspan membrane glycoprotein, not a truncated form as previously reported. This study confirms the correct structure of rat prominin, essential for understanding its biological functions.

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • Prominin is a novel family of membrane glycoproteins with a characteristic five transmembrane segment topology.
  • Orthologues and paralogues of prominin exist across various species, including mammals, fish, flies, and worms.
  • A previous report suggested rat prominin is a truncated form due to a frameshift mutation in its cDNA.

Purpose of the Study:

  • To investigate and clarify the true structure of rat prominin.
  • To determine if rat prominin is a full-length pentaspan glycoprotein or a C-terminally truncated form.
  • To provide accurate molecular data on rat prominin.

Main Methods:

  • Isolation of rat prominin cDNA.
  • DNA sequencing to identify mutations.
  • Protein characterization and molecular weight determination.
  • Detection of truncated protein forms.

Main Results:

  • A rat prominin cDNA sequence devoid of frameshift mutations was isolated.
  • Rat prominin was demonstrated to be a full-length 120-kDa pentaspan membrane glycoprotein.
  • No evidence for a C-terminally truncated form of rat prominin was detected.

Conclusions:

  • The previous report of a truncated rat prominin was incorrect.
  • Rat prominin shares the full-length pentaspan structure with other mammalian prominins.
  • This finding corrects the molecular understanding of rat prominin.

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