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Updated: Jun 14, 2026

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay
Published on: May 26, 2011
CMTM5-v1, a four-transmembrane protein, presents a secreted form released via a vesicle-mediated secretory pathway
Henan Li1, Xiaohuan Guo, Luning Shao
1Center for Human Disease Genomics, Department of Immunology, School of Basic Medical Sciences, Health Science Center, Peking University, 38 Xueyuan Road, Beijing 100191, China.
Abstract:
The CKLF-like MARVEL transmembrane domain-containing family (CMTM) is a novel family of proteins linking classical chemokines and the transmembrane 4 superfamily (TM4SF). Our earlier studies indicated several CMTM members (such as CKLF1 and CMTM2) have a secreted form. This is the first report of the secreted form of CMTM5-v1, the major RNA splicing form of CMTM5, which is produced as small vesicles (100 nm diameter) and floats at a peak density of 1.19 g/ml on continuous sucrose gradients. CMTM5-v1 has no obvious co-localization with CD63 or Golgi complex. In addition, brefeldin A but not wortmannin can inhibit the secretion of CMTM5-v1. Our results suggest that CMTM5-v1 might be secreted via a different vesicle-mediated secretory pathway, which will be helpful for the studies of vesicle-mediated secretion and MARVEL domain-containing proteins.
Insights
This study reports the first evidence of a secreted form of CMTM5-v1, a protein involved in cell communication. This novel secretion pathway offers insights into vesicle-mediated transport mechanisms.
Area of Science:
- Molecular Biology
- Cell Biology
- Biochemistry
Background:
- The CKLF-like MARVEL transmembrane domain-containing (CMTM) family links chemokines and TM4SF proteins.
- Previous research identified secreted forms of CMTM1 and CMTM2.
- CMTM5-v1 is the primary RNA splicing variant of CMTM5.
Purpose of the Study:
- To characterize the secreted form of CMTM5-v1.
- To investigate the secretion pathway of CMTM5-v1.
- To explore the implications for vesicle-mediated secretion research.
Main Methods:
- Sucrose gradient ultracentrifugation to determine vesicle density.
- Immunofluorescence microscopy to assess co-localization with markers (CD63, Golgi).
- Pharmacological inhibition of secretion pathways using brefeldin A and wortmannin.
Main Results:
- CMTM5-v1 is secreted in small vesicles (100 nm diameter) with a peak density of 1.19 g/ml.
- CMTM5-v1 does not co-localize with CD63 or the Golgi complex.
- Secretion of CMTM5-v1 is inhibited by brefeldin A but not wortmannin.
Conclusions:
- CMTM5-v1 is secreted via a distinct vesicle-mediated pathway.
- This finding contributes to understanding MARVEL domain protein secretion.
- The study opens new avenues for research into unconventional secretory mechanisms.
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