title: Expression and characterization of transmembrane and coiled-coil domain family 3.
abstract: Transmembrane and coiled-coil domain family 3 (TMCC3) has been reported to be expressed in the human brain; however, its function is still unknown. Here, we found that expression of TMCC3 is higher in human whole brain, testis and spinal cord compared to other human tissues. TMCC3 was expressed in mouse developing hind brain, lung, kidney and somites, with strongest expression in the mesenchyme of developing tongue. By expression of recombinant TMCC3 and its deletion mutants, we found that TMCC3 proteins self-assemble to oligomerize. Immunostaining and confocal microscopy data revealed that TMCC3 proteins are localized in endoplasmic reticulum through transmembrane domains. Based on immunoprecipitation and mass spectroscopy data, TMCC3 proteins associate with TMCC3 and 14-3-3 proteins. This supports the idea that TMCC3 proteins form oligomers and that 14-3-3 may be involved in the function of TMCC3. Taken together, these results may be useful for better understanding of uncharacterized function of TMCC3. [BMB Reports 2016; 49(11): 629-634].
authors.affiliation: Department of Biochemistry, School of Dentistry, IHBR, Kyungpook National University, Daegu 41940, Korea.
authors.forename: Wern-Joo
authors.initials: WJ
authors.lastname: Sohn
authors.affiliation: Department of Biochemistry, School of Dentistry, IHBR, Kyungpook National University, Daegu 41940, Korea.
authors.forename: Jae-Young
authors.initials: JY
authors.lastname: Kim
authors.affiliation: Center for Medical Science Research, College of Medicine, Hallym University, Chuncheon 24252, Korea.
authors.forename: Dongbum
authors.initials: D
authors.lastname: Kim
authors.affiliation: Department of Biochemistry, College of Natural Sciences, Chungbuk National University, Cheongju 28644, Korea.
authors.forename: Jeong-A
authors.initials: JA
authors.lastname: Park
authors.affiliation: Department of Biochemistry, College of Natural Sciences, Chungbuk National University, Cheongju 28644, Korea.
authors.forename: Younghee
authors.initials: Y
authors.lastname: Lee
authors.affiliation: Center for Medical Science Research, College of Medicine, Hallym University, Chuncheon 24252; Department of Microbiology, College of Medicine, Hallym University, Chuncheon 24252, Korea.
authors.forename: Hyung-Joo
authors.initials: HJ
authors.lastname: Kwon
mesh_terms: D048948:14-3-3 Proteins / Q000737:chemistry / Q000378:metabolism; D000818:Animals; D015153:Blotting, Western; D001921:Brain / Q000378:metabolism; D004622:Embryo, Mammalian / Q000378:metabolism; D005260:Female; D057809:HEK293 Cells; D006801:Humans; D047468:Immunoprecipitation; D017403:In Situ Hybridization; D008297:Male; D008565:Membrane Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D051379:Mice; D008813:Mice, Inbred ICR; D008856:Microscopy, Fluorescence; D016296:Mutagenesis; D016376:Oligonucleotides, Antisense / Q000378:metabolism; D055503:Protein Multimerization; D060888:Real-Time Polymerase Chain Reaction; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000737:chemistry / Q000302:isolation & purification
chemical_list: D048948:14-3-3 Proteins; C432970:HHATL protein, human; D008565:Membrane Proteins; D016376:Oligonucleotides, Antisense; D011994:Recombinant Proteins