TY - JOUR
T1 - Interaction between a plasma membrane-localized ankyrin-repeat protein ITN1 and a nuclear protein RTV1
AU - Sakamoto, Hikaru
AU - Sakata, Keiko
AU - Kusumi, Kensuke
AU - Kojima, Mikiko
AU - Sakakibara, Hitoshi
AU - Iba, Koh
N1 - Funding Information:
We thank Dr. Nir Ohad (Tel-Aviv University) and Dr. Yutaka Kodama (Utsunomiya University) for providing vectors pSY735, pSY736 and CFP, the Arabidopsis Biological Resource Center for providing the SALK_131754 line and the Arabidopsis cDNA library (CD4-10). This work was supported by a Grant-in-Aid for Scientific Research on Innovative Areas (No. 21114002 ) from the Ministry of Education, Science and Culture of Japan , and by the Program for Promotion of Basic and Applied Researches for Innovations in Bio-oriented Industry (BRAIN).
PY - 2012/6/29
Y1 - 2012/6/29
N2 - The increased tolerance to NaCl 1 (ITN1) protein is a plasma membrane (PM)-localized protein involved in responses to NaCl stress in Arabidopsis. The predicted structure of ITN1 is composed of multiple transmembrane regions and an ankyrin-repeat domain that is known to mediate protein-protein interactions. To elucidate the molecular functions of ITN1, we searched for interacting partners using a yeast two-hybrid assay, and a nuclear-localized DNA-binding protein, RTV1, was identified as a candidate. Bimolecular fluorescence complementation analysis revealed that RTV1 interacted with ITN1 at the PM and nuclei in vivo. RTV1 tagged with red fluorescent protein localized to nuclei and ITN1 tagged with green fluorescent protein localized to PM; however, both proteins localized to both nuclei and the PM when co-expressed. These findings suggest that RTV1 and ITN1 regulate the subcellular localization of each other.
AB - The increased tolerance to NaCl 1 (ITN1) protein is a plasma membrane (PM)-localized protein involved in responses to NaCl stress in Arabidopsis. The predicted structure of ITN1 is composed of multiple transmembrane regions and an ankyrin-repeat domain that is known to mediate protein-protein interactions. To elucidate the molecular functions of ITN1, we searched for interacting partners using a yeast two-hybrid assay, and a nuclear-localized DNA-binding protein, RTV1, was identified as a candidate. Bimolecular fluorescence complementation analysis revealed that RTV1 interacted with ITN1 at the PM and nuclei in vivo. RTV1 tagged with red fluorescent protein localized to nuclei and ITN1 tagged with green fluorescent protein localized to PM; however, both proteins localized to both nuclei and the PM when co-expressed. These findings suggest that RTV1 and ITN1 regulate the subcellular localization of each other.
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U2 - 10.1016/j.bbrc.2012.05.136
DO - 10.1016/j.bbrc.2012.05.136
M3 - Article
C2 - 22664102
AN - SCOPUS:84862851686
SN - 0006-291X
VL - 423
SP - 392
EP - 397
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 2
ER -