ArticleMolecular and cellular biology2007
Btn2, a Hook1 ortholog and potential Batten disease-related protein, mediates late endosome-Golgi protein sorting in yeast.
Article in Molecular and cellular biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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39 citing papers in PubMed, 78 citations in OpenAlex.
- Endocytosis and trans-Golgi Network in Yeast.Sub-cellular biochemistry · 2026Review
- Anti-Prion Systems in Saccharomyces cerevisiae.Journal of neurochemistry · 2025Review
- Lysosomal positioning diseases: beyond substrate storage.Open biology · 2022Review
- Innate immunity to prions: anti-prion systems turn a tsunami of prions into a slow drip.Current genetics · 2021Review
- Sorting Out Sorting Nexins Functions in the Nervous System in Health and Disease.Molecular neurobiology · 2021Review
- Article
- Understanding the Impact of Industrial Stress Conditions on Replicative Aging inFrontiers in fungal biology · 2021Review
- Cellular models of Batten disease.Biochimica et biophysica acta. Molecular basis of disease · 2020Review
- How Do Yeast Cells Contend with Prions?International journal of molecular sciences · 2020Review
- Review
- Anti-prion systems in yeast.The Journal of biological chemistry · 2019Review
- Transcriptional profiling of Zygosaccharomyces bailii early response to acetic acid or copper stress mediated by ZbHaa1.Scientific reports · 2018Article
- Cdc48 and ubiquilins confer selective anterograde protein sorting and entry into the multivesicular body in yeast.Molecular biology of the cell · 2018Article
- Anti-Prion Systems in Yeast and Inositol Polyphosphates.Biochemistry · 2018Article
- Yeast and Fungal Prions.Cold Spring Harbor perspectives in biology · 2016Review
- Prioritized Expression of BTN2 of Saccharomyces cerevisiae under Pronounced Translation Repression Induced by Severe Ethanol Stress.Frontiers in microbiology · 2016Article
- Yeast and Fungal Prions: Amyloid-Handling Systems, Amyloid Structure, and Prion Biology.Advances in genetics · 2016Article
- Expression of three topologically distinct membrane proteins elicits unique stress response pathways in the yeast Saccharomyces cerevisiae.Physiological genomics · 2015Article
- Spatiotemporal dynamics of membrane remodeling and fusion proteins during endocytic transport.Molecular biology of the cell · 2015Article
- Yeast prions: structure, biology, and prion-handling systems.Microbiology and molecular biology reviews : MMBR · 2015Review
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
BTN2 gene expression in the yeast Saccharomyces cerevisiae is up-regulated in response to the deletion of BTN1, which encodes the ortholog of a human Batten disease protein. We isolated Btn2 as a Snc1 v-SNARE binding protein using the two-hybrid assay and examined its role in intracellular protein trafficking. We show that Btn2 is an ortholog of the Drosophila and mammalian Hook1 proteins that interact with SNAREs, cargo proteins, and coat components involved in endosome-Golgi protein sorting. By immunoprecipitation, it was found that Btn2 bound the yeast endocytic SNARE complex (e.g., Snc1 and Snc2 [Snc1/2], Tlg1, Tlg2, and Vti1), the Snx4 sorting nexin, and retromer (e.g., Vps26 and Vps35). In in vitro binding assays, recombinant His(6)-tagged Btn2 bound glutathione S-transferase (GST)-Snc1 and GST-Vps26. Btn2-green fluorescent protein and Btn2-red fluorescent protein colocalize with Tlg2, Snx4, and Vps27 to a compartment adjacent to the vacuole that corresponds to a late endosome. The deletion of BTN2 blocks Yif1 retrieval back to the Golgi apparatus, while the localization of Ste2, Fur4, Snc1, Vps10, carboxypeptidases Y (CPY) and S (CPS), Sed5, and Sec7 is unaltered in btn2Delta cells. Yif1 delivery to the vacuole was observed in other late endosome-Golgi trafficking mutants, including ypt6Delta, snx4Delta, and vps26Delta cells. Thus, Btn2 facilitates specific protein retrieval from a late endosome to the Golgi apparatus, a process which may be adversely affected in patients with Batten disease.
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