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. 2000 Feb 7;148(3):453–464. doi: 10.1083/jcb.148.3.453

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© 2000 The Rockefeller University Press

This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).

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A model of protein mobilization in the cotyledon cell of germinated V. mungo seeds. The digestion of storage proteins in germinated cotyledons occurs in cells farthest from the vascular bundle (VB). The proform of SH-EP synthesized in the lumen of ER is packed into the KDEL-tailed cysteine proteinase-accumulating vesicle (KV) at the edge or the middle region of ER, and KV (200–500 nm in diameter) filled with proSH-EP, buds off from ER, bypasses the Golgi complex and fuses with PSV, resulting in the release of proSH-EP into the inside of PSV. A large amount of proSH-EP sorted to PSV is converted to the mature enzyme by autocatalytic and/or VmPE-1–mediated fashions, and the activated mature SH-EP massively degrades the storage globulin. This process mediates the change of the cotyledon cells filled with storage proteins (shaded cells) to vacuolized cells (non-shaded cells). ER, endoplasmic reticulum; G, Golgi complex; KV, KDEL-tailed cysteine proteinase-accumulating vesicle; PSV, protein storage vacuole; VB, vascular bundle; PSV1, protein storage vacuole filled with proteins; PSV2, vacuole in which storage proteins were degraded.