2023
DOI: 10.1063/5.0176048
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Metalation and activation of Zn2+ enzymes via early secretory pathway-resident ZNT proteins

Taiho Kambe,
Takumi Wagatsuma

Abstract: Zinc (Zn2+), an essential trace element, binds to various proteins, including enzymes, transcription factors, channels, and signaling molecules and their receptors, to regulate their activities in a wide range of physiological functions. Zn2+ proteome analyses have indicated that approximately 10% of the proteins encoded by the human genome have potential Zn2+ binding sites. Zn2+ binding to the functional site of a protein (for enzymes, the active site) is termed Zn2+ metalation. In eukaryotic cells, approxima… Show more

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Cited by 3 publications
(1 citation statement)
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“…ZnT7 and ZnT5/6 are responsible for the Golgi-to-ER retrograde transport of the ER chaperone ERp44 [ 64 ]. This system is involved in the maturation and activation of some secretory proteins during transport through the early secretory pathway [ 65 ].…”
Section: Zntsmentioning
confidence: 99%
“…ZnT7 and ZnT5/6 are responsible for the Golgi-to-ER retrograde transport of the ER chaperone ERp44 [ 64 ]. This system is involved in the maturation and activation of some secretory proteins during transport through the early secretory pathway [ 65 ].…”
Section: Zntsmentioning
confidence: 99%