한빛사 논문
Yun Kwona, Jinbo Shenb, Myoung Hui Leec, Kyoung Rok Geema, Liwen Jiangb,d, and Inhwan Hwanga,c,1
aDepartment of Life Sciences, Pohang University of Science and Technology, 37673 Pohang, Korea; bState Key Laboratory of Agrobiotechnology, Centre for Cell and Developmental Biology, School of Life Sciences, The Chinese University of Hong Kong, Shatin, New Territories, Hong Kong, China; cDivision of Integrative Biosciences and Biotechnology, Pohang University of Science and Technology, 37673 Pohang, Korea; and dCUHK Shenzhen Research Institute, The Chinese University of Hong Kong, 518057 Shenzhen, China
1To whom correspondence should be addressed.
Abstract
Protein trafficking is a fundamental mechanism of subcellular organization and contributes to organellar biogenesis. AtCAP2 is an Arabidopsis homolog of the Mesembryanthemum crystallinum calcium-dependent protein kinase 1 adaptor protein 2 (McCAP2), a member of the syntaxin superfamily. Here, we show that AtCAP2 plays an important role in the conversion to the lytic vacuole (LV) during early plant development. The AtCAP2 loss-of-function mutant atcap2-1 displayed delays in protein storage vacuole (PSV) protein degradation, PSV fusion, LV acidification, and biosynthesis of several vacuolar proteins during germination. At the mature stage, atcap2-1 plants accumulated vacuolar proteins in the prevacuolar compartment (PVC) instead of the LV. In wild-type plants, AtCAP2 localizes to the PVC as a peripheral membrane protein and in the PVC compartment recruits glyceraldehyde-3-phosphate dehydrogenase C2 (GAPC2) to the PVC. We propose that AtCAP2 contributes to LV biogenesis during early plant development by supporting the trafficking of specific proteins involved in the PSV-to-LV transition and LV acidification during early stages of plant development.
lytic vacuole transition, vacuolar pH, vacuolar trafficking, intracellular trafficking, GAPC2 trafficking
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