Journal
PLANT PHYSIOLOGY
Volume 166, Issue 1, Pages 125-138Publisher
AMER SOC PLANT BIOLOGISTS
DOI: 10.1104/pp.114.240945
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Funding
- Belgian National Fund for Scientific Research
- Interuniversity Attraction Poles Programme-Belgian Science Policy
- Communaute francaise de Belgique-Actions de Recherches Concertees
- Francqui Foundation
- Bauchau Award
- Fonds de Formation a la Recherche dans l'Industrie et l'Agriculture [FC89796]
- individual Marie Curie European Fellowship
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Aquaporins play important roles in maintaining plant water status under challenging environments. The regulation of aquaporin density in cell membranes is essential to control transcellular water flows. This work focuses on the maize (Zea mays) plasma membrane intrinsic protein (ZmPIP) aquaporin subfamily, which is divided into two sequence-related groups (ZmPIP1s and ZmPIP2s). When expressed alone in mesophyll protoplasts, ZmPIP2s are efficiently targeted to the plasma membrane, whereas ZmPIP1s are retained in the endoplasmic reticulum (ER). A protein domain-swapping approach was utilized to demonstrate that the transmembrane domain3 (TM3), together with the previously identified N-terminal ER export diacidic motif, account for the differential localization of these proteins. In addition to protoplasts, leaf epidermal cells transiently transformed by biolistic particle delivery were used to confirm and refine these results. By generating artificial proteins consisting of a single transmembrane domain, we demonstrated that the TM3 of ZmPIP1; 2 or ZmPIP2; 5 discriminates between ER and plasma membrane localization, respectively. More specifically, a new LxxxA motif in the TM3 of ZmPIP2; 5, which is highly conserved in plant PIP2s, was shown to regulate its anterograde routing along the secretory pathway, particularly its export from the ER.
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