Demonstration and Characterization of the Heterodimerization of ZnT5 and ZnT6 in the Early Secretory Pathway

• Published in: The Journal of biological chemistry Vol. 284; no. 45; pp. 30798 - 30806
• Main Authors: Fukunaka, Ayako, Suzuki, Tomoyuki, Kurokawa, Yayoi, Yamazaki, Tomohiro, Fujiwara, Naoko, Ishihara, Kaori, Migaki, Hitoshi, Okumura, Katsuzumi, Masuda, Seiji, Yamaguchi-Iwai, Yuko, Nagao, Masaya, Kambe, Taiho
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 06.11.2009; American Society for Biochemistry and Molecular Biology
• Subjects: Amino Acid Motifs; Amino Acid Sequence; Animals; Cation Transport Proteins - chemistry; Cation Transport Proteins - genetics; Cation Transport Proteins - metabolism; Cell Line; Chickens; Dimerization; Humans; Membrane Transport, Structure, Function, and Biogenesis; Molecular Sequence Data; Protein Binding; Secretory Pathway; Sequence Alignment

The majority of CDF/ZnT zinc transporters form homo-oligomers. However, ZnT5, ZnT6, and their orthologues form hetero-oligomers in the early secretory pathway where they load zinc onto zinc-requiring enzymes and maintain secretory pathway functions. The details of this hetero-oligomerization remain...