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Updated: Jul 27, 2026

Membrane-SPINE: A Biochemical Tool to Identify Protein-protein Interactions of Membrane Proteins In Vivo
Published on: November 7, 2013
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.
Abstract:
Mouse prominin is the first characterized member of a novel family of membrane glycoproteins. It displays a characteristic membrane topology with five transmembrane segments and two large glycosylated extracellular loops. Prominin orthologues and paralogues have been identified in human, fish, fly, and worm. Recently, a cDNA sequence encoding the rat homologue of mouse prominin has been reported [Zhu et al. (2001) Biochem. Biophys. Res. Commun. 281, 951-956]. Surprisingly, due to a single nucleotide deletion that shifts the reading frame and introduces a premature stop codon, the protein predicted from this cDNA would correspond to a C-terminally truncated form of prominin with only four transmembrane segments. Here we report evidence that is in contrast to the report of Zhu et al. (2001). We isolated a rat prominin cDNA devoid of any frameshift mutation, demonstrate that rat prominin, like the other mammalian prominins, is a full-length 120-kDa pentaspan membrane glycoprotein, and have not been able to detect any C-terminally truncated form of rat prominin.
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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