ArticleJournal of cell science2015
TM9 family proteins control surface targeting of glycine-rich transmembrane domains.
Article in Journal of cell science, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 23 citations in OpenAlex.
- Characterization of Exosome-like Nanoparticles from Saffron Tepals and Their Immunostimulatory Activity.Biology · 2025Article
- Compound K14 inhibits bacterial killing and protease activity in Dictyostelium discoideum phagosomes.PloS one · 2024Article
- A CRISPR screen in intestinal epithelial cells identifies novel factors for polarity and apical transport.eLife · 2023Article
- Genome-wide analysis of transmembrane 9 superfamily genes in wheat (Frontiers in plant science · 2023Article
- TM9SF4 is an F-actin disassembly factor that promotes tumor progression and metastasis.Nature communications · 2022Article
- Golgi-localized membrane protein AtTMN1/EMP12 functions in the deposition of rhamnogalacturonan II and I for cell growth in Arabidopsis.Journal of experimental botany · 2021Article
- Whole-exome sequencing reveals ANO8 as a genetic risk factor for intrahepatic cholestasis of pregnancy.BMC pregnancy and childbirth · 2020Article
- Transposon mutagenesis screen in mice identifies TM9SF2 as a novel colorectal cancer oncogene.Scientific reports · 2018Article
- CRISPR Screen Reveals that EHEC's T3SS and Shiga Toxin Rely on Shared Host Factors for Infection.mBio · 2018Article
- Role of the HIV-1 envelope transmembrane domain in intracellular sorting.BMC cell biology · 2018Article
- TM9SF4 is a novel factor promoting autophagic flux under amino acid starvation.Cell death and differentiation · 2018Article
- MitoNEET-dependent formation of intermitochondrial junctions.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- APP Receptor? To Be or Not To Be.Trends in pharmacological sciences · 2016Review
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
TM9 family proteins (also named Phg1 proteins) have been previously shown to control cell adhesion by determining the cell surface localization of adhesion proteins such as the Dictyostelium SibA protein. Here, we show that the glycine-rich transmembrane domain (TMD) of SibA is sufficient to confer Phg1A-dependent surface targeting to a reporter protein. Accordingly, in Dictyostelium phg1A-knockout (KO) cells, proteins with glycine-rich TMDs were less efficiently transported out of the endoplasmic reticulum (ER) and to the cell surface. Phg1A, as well as its human ortholog TM9SF4 specifically associated with glycine-rich TMDs. In human cells, genetic inactivation of TM9SF4 resulted in an increased retention of glycine-rich TMDs in the endoplasmic reticulum, whereas TM9SF4 overexpression enhanced their surface localization. The bulk of the TM9SF4 protein was localized in the Golgi complex and a proximity-ligation assay suggested that it might interact with glycine-rich TMDs. Taken together, these results suggest that one of the main roles of TM9 proteins is to serve as intramembrane cargo receptors controlling exocytosis and surface localization of a subset of membrane proteins.
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