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Elife. 2014 Apr 8;3:e02131. doi: 10.7554/eLife.02131.

Delivery of endocytosed proteins to the cell-division plane requires change of pathway from recycling to secretion.

Author information

1
Department of Developmental Genetics, The Center for Plant Molecular Biology (ZMBP), University of Tübingen, Tübingen, Germany.

Abstract

Membrane trafficking is essential to fundamental processes in eukaryotic life, including cell growth and division. In plant cytokinesis, post-Golgi trafficking mediates a massive flow of vesicles that form the partitioning membrane but its regulation remains poorly understood. Here, we identify functionally redundant Arabidopsis ARF guanine-nucleotide exchange factors (ARF-GEFs) BIG1-BIG4 as regulators of post-Golgi trafficking, mediating late secretion from the trans-Golgi network but not recycling of endocytosed proteins to the plasma membrane, although the TGN also functions as an early endosome in plants. In contrast, BIG1-4 are absolutely required for trafficking of both endocytosed and newly synthesized proteins to the cell-division plane during cytokinesis, counteracting recycling to the plasma membrane. This change from recycling to secretory trafficking pathway mediated by ARF-GEFs confers specificity of cargo delivery to the division plane and might thus ensure that the partitioning membrane is completed on time in the absence of a cytokinesis-interphase checkpoint. DOI: http://dx.doi.org/10.7554/eLife.02131.001.

KEYWORDS:

ARF-GEF; cell division; gegulation of vesicle traffic; post-Golgi trafficking; recycling; secretion

PMID:
24714496
PMCID:
PMC3979144
DOI:
10.7554/eLife.02131
[Indexed for MEDLINE]
Free PMC Article

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