Premium
TMD1 domain and CRAC motif determine the association and disassociation of MxIRT1 with detergent‐resistant membranes
Author(s) -
Tan Song,
Zhang Peng,
Xiao Wei,
Feng Bing,
Chen LanYou,
Li Shuang,
Li Peng,
Zhao WeiZhong,
Qi XiaoTing,
Yin LiPing
Publication year - 2018
Publication title -
traffic
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.677
H-Index - 130
eISSN - 1600-0854
pISSN - 1398-9219
DOI - 10.1111/tra.12540
Subject(s) - endoplasmic reticulum , biology , copii , microbiology and biotechnology , transmembrane domain , intracellular , membrane , transport protein , signal transduction , vesicle , biochemistry , golgi apparatus , secretory pathway
Iron is essential for most living organisms. The iron‐regulated transporter1 (IRT1) plays a major role in iron uptake in roots, and its trafficking from endoplasmic reticulum (ER) to plasma membrane (PM) is tightly coordinated with changes in iron environment. However, studies on the IRT1 response are limited. Here, we report that Malus xiaojinesis IRT1 (MxIRT1) associates with detergent‐resistant membranes (DRMs, a biochemical counterpart of PM microdomains), whereas the PM microdomains are known platforms for signal transduction in the PM. Depending on the shift of MxIRT1 from microdomains to homogeneous regions in PM, MxIRT1‐mediated iron absorption is activated by the cholesterol recognition/interaction amino acid consensus (CRAC) motif of MxIRT1. MxIRT1 initially associates with DRMs in ER via its transmembrane domain 1 (TMD1), and thus begins DRMs‐dependent intracellular trafficking. Subsequently, MxIRT1 is sequestered in COPII vesicles via the ER export signal sequence in MxIRT1. These studies suggest that iron homeostasis is influenced by the CRAC motif and TMD1 domain due to their determination of MxIRT1‐DRMs association.