The histidine-rich loop in the extracellular domain of ZIP4 binds zinc and plays a role in zinc transport.

ABSTRACT: The Zrt-/Irt-like protein (ZIP) family mediates zinc influx from extracellular space or intracellular vesicles/organelles, playing a central role in systemic and cellular zinc homeostasis. Out of the 14 family members encoded in human genome, ZIP4 is exclusively responsible for zinc uptake from dietary food and dysfunctional mutations of ZIP4 cause a life-threatening genetic disorder, Acrodermatitis Enteropathica (AE). About half of the missense AE-causing mutations occur within the large N-terminal extracellular domain (ECD), and our previous study has shown that ZIP4-ECD is crucial for optimal zinc uptake but the underlying mechanism has not been clarified. In this work, we examined zinc binding to the isolated ZIP4-ECD from Pteropus Alecto (black fruit bat) and located zinc-bindi

SUBMITTER: Zhang T 

PROVIDER: S-EPMC7661218 | biostudies-literature | 2019 Jun

REPOSITORIES: biostudies-literature