Molecular Characterization of Mammalian Homologues of Class C Vps Proteins That Interact with Syntaxin-7

Bong Yoon Kim, Helmut Krämer, Akitsugu Yamamoto, Eiki Kominami, Shinichi Kohsaka, Chihiro Akazawa

Research output: Contribution to journalArticle

63 Citations (Scopus)

Abstract

Vesicle-mediated protein sorting plays an important role in segregation of intracellular molecules into distinct organelles. Extensive genetic studies using yeast have identified more than 40 vacuolar protein sorting (VPS) genes involved in vesicle transport to vacuoles. However, their mammalian counterparts are not fully elucidated. In this study, we identified two human homologues of yeast Class C VPS genes, human VPS11 (hVPS11) and human VPS18 (hVPS18). We also characterized the subcellular localization and interactions of the protein products not only from these genes but also from the other mammalian Class C VPS homologue genes, hVPS16 and rVPS33a. The protein products of hVPS11 (hVps11) and hVPS18 (hVps18) were ubiquitously expressed in peripheral tissues, suggesting that they have a fundamental role in cellular function. Indirect immunofluorescence microscopy revealed that the mammalian Class C Vps proteins are predominantly associated with late endosomes/lysosomes. Immunoprecipitation and gel filtration studies showed that the mammalian Class C Vps proteins constitute a large hetero-oligomeric complex that interacts with syntaxin-7. These results indicate that like their yeast counterparts, mammalian Class C Vps proteins mediate vesicle trafficking steps in the endosome/lysosome pathway.

Original languageEnglish (US)
Pages (from-to)29393-29402
Number of pages10
JournalJournal of Biological Chemistry
Volume276
Issue number31
DOIs
StatePublished - Aug 3 2001

Fingerprint

Qa-SNARE Proteins
Protein Transport
Protein C
Yeasts
Endosomes
Lysosomes
Genes
Sorting
Proteins
Transport Vesicles
Yeast
Indirect Fluorescent Antibody Technique
Vacuoles
Fluorescence Microscopy
Immunoprecipitation
Organelles
Gel Chromatography
Microscopic examination
Gels
Tissue

ASJC Scopus subject areas

  • Biochemistry

Cite this

Molecular Characterization of Mammalian Homologues of Class C Vps Proteins That Interact with Syntaxin-7. / Kim, Bong Yoon; Krämer, Helmut; Yamamoto, Akitsugu; Kominami, Eiki; Kohsaka, Shinichi; Akazawa, Chihiro.

In: Journal of Biological Chemistry, Vol. 276, No. 31, 03.08.2001, p. 29393-29402.

Research output: Contribution to journalArticle

Kim, Bong Yoon ; Krämer, Helmut ; Yamamoto, Akitsugu ; Kominami, Eiki ; Kohsaka, Shinichi ; Akazawa, Chihiro. / Molecular Characterization of Mammalian Homologues of Class C Vps Proteins That Interact with Syntaxin-7. In: Journal of Biological Chemistry. 2001 ; Vol. 276, No. 31. pp. 29393-29402.
@article{a835826901074b20a638e5bdfa11f1fe,
title = "Molecular Characterization of Mammalian Homologues of Class C Vps Proteins That Interact with Syntaxin-7",
abstract = "Vesicle-mediated protein sorting plays an important role in segregation of intracellular molecules into distinct organelles. Extensive genetic studies using yeast have identified more than 40 vacuolar protein sorting (VPS) genes involved in vesicle transport to vacuoles. However, their mammalian counterparts are not fully elucidated. In this study, we identified two human homologues of yeast Class C VPS genes, human VPS11 (hVPS11) and human VPS18 (hVPS18). We also characterized the subcellular localization and interactions of the protein products not only from these genes but also from the other mammalian Class C VPS homologue genes, hVPS16 and rVPS33a. The protein products of hVPS11 (hVps11) and hVPS18 (hVps18) were ubiquitously expressed in peripheral tissues, suggesting that they have a fundamental role in cellular function. Indirect immunofluorescence microscopy revealed that the mammalian Class C Vps proteins are predominantly associated with late endosomes/lysosomes. Immunoprecipitation and gel filtration studies showed that the mammalian Class C Vps proteins constitute a large hetero-oligomeric complex that interacts with syntaxin-7. These results indicate that like their yeast counterparts, mammalian Class C Vps proteins mediate vesicle trafficking steps in the endosome/lysosome pathway.",
author = "Kim, {Bong Yoon} and Helmut Kr{\"a}mer and Akitsugu Yamamoto and Eiki Kominami and Shinichi Kohsaka and Chihiro Akazawa",
year = "2001",
month = "8",
day = "3",
doi = "10.1074/jbc.M101778200",
language = "English (US)",
volume = "276",
pages = "29393--29402",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "31",

}

TY - JOUR

T1 - Molecular Characterization of Mammalian Homologues of Class C Vps Proteins That Interact with Syntaxin-7

AU - Kim, Bong Yoon

AU - Krämer, Helmut

AU - Yamamoto, Akitsugu

AU - Kominami, Eiki

AU - Kohsaka, Shinichi

AU - Akazawa, Chihiro

PY - 2001/8/3

Y1 - 2001/8/3

N2 - Vesicle-mediated protein sorting plays an important role in segregation of intracellular molecules into distinct organelles. Extensive genetic studies using yeast have identified more than 40 vacuolar protein sorting (VPS) genes involved in vesicle transport to vacuoles. However, their mammalian counterparts are not fully elucidated. In this study, we identified two human homologues of yeast Class C VPS genes, human VPS11 (hVPS11) and human VPS18 (hVPS18). We also characterized the subcellular localization and interactions of the protein products not only from these genes but also from the other mammalian Class C VPS homologue genes, hVPS16 and rVPS33a. The protein products of hVPS11 (hVps11) and hVPS18 (hVps18) were ubiquitously expressed in peripheral tissues, suggesting that they have a fundamental role in cellular function. Indirect immunofluorescence microscopy revealed that the mammalian Class C Vps proteins are predominantly associated with late endosomes/lysosomes. Immunoprecipitation and gel filtration studies showed that the mammalian Class C Vps proteins constitute a large hetero-oligomeric complex that interacts with syntaxin-7. These results indicate that like their yeast counterparts, mammalian Class C Vps proteins mediate vesicle trafficking steps in the endosome/lysosome pathway.

AB - Vesicle-mediated protein sorting plays an important role in segregation of intracellular molecules into distinct organelles. Extensive genetic studies using yeast have identified more than 40 vacuolar protein sorting (VPS) genes involved in vesicle transport to vacuoles. However, their mammalian counterparts are not fully elucidated. In this study, we identified two human homologues of yeast Class C VPS genes, human VPS11 (hVPS11) and human VPS18 (hVPS18). We also characterized the subcellular localization and interactions of the protein products not only from these genes but also from the other mammalian Class C VPS homologue genes, hVPS16 and rVPS33a. The protein products of hVPS11 (hVps11) and hVPS18 (hVps18) were ubiquitously expressed in peripheral tissues, suggesting that they have a fundamental role in cellular function. Indirect immunofluorescence microscopy revealed that the mammalian Class C Vps proteins are predominantly associated with late endosomes/lysosomes. Immunoprecipitation and gel filtration studies showed that the mammalian Class C Vps proteins constitute a large hetero-oligomeric complex that interacts with syntaxin-7. These results indicate that like their yeast counterparts, mammalian Class C Vps proteins mediate vesicle trafficking steps in the endosome/lysosome pathway.

UR - http://www.scopus.com/inward/record.url?scp=0035800740&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0035800740&partnerID=8YFLogxK

U2 - 10.1074/jbc.M101778200

DO - 10.1074/jbc.M101778200

M3 - Article

C2 - 11382755

AN - SCOPUS:0035800740

VL - 276

SP - 29393

EP - 29402

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 31

ER -