PMID- 31396242
OWN - NLM
STAT- PubMed-not-MEDLINE
LR  - 20220409
IS  - 1664-462X (Print)
IS  - 1664-462X (Electronic)
IS  - 1664-462X (Linking)
VI  - 10
DP  - 2019
TI  - Tethering of Multi-Vesicular Bodies and the Tonoplast to the Plasma Membrane in 
      Plants.
PG  - 636
LID - 10.3389/fpls.2019.00636 [doi]
LID - 636
AB  - Tethering of the plasma membrane (PM) and many organelles to the endoplasmic 
      reticulum (ER) for communication and lipid exchange has been widely reported. 
      However, despite growing interest in multi-vesicular bodies (MVBs) as possible 
      sources of exosomes, tethering of MVBs to the PM has not been reported. Here we 
      show that MVBs and the vacuolar membrane (tonoplast) could be tethered to the PM 
      (PM-MVB/TP tethering) by artificial protein fusions or bimolecular fluorescence 
      complementation (BiFC) complexes that contain a peripheral membrane protein that 
      binds the PM and also a protein that binds MVBs or the tonoplast. PM-binding 
      proteins capable of participating in PM-MVB/TP tethering included StRem1.3, BIK1, 
      PBS1, CPK21, and the PtdIns(4)-binding proteins FAPP1 and Osh2. MVB/TP-binding 
      proteins capable of participating in tethering included ARA6, ARA7, RHA1, RABG3f, 
      and the PtdIns(3)P-binding proteins Vam7p and Hrs-2xFYVE. BiFC complexes or 
      protein fusions capable of producing PM-MVB/TP tethering were visualized as large 
      well-defined patches of fluorescence on the PM that could displace PM proteins 
      such as AtFlotillin1 and also could displace cytoplasmic proteins such as soluble 
      GFP. Furthermore, we identified paralogous ubiquitin E3 ligase proteins, SAUL1 
      (AtPUB44), and AtPUB43 that could produce PM-MVB/TP tethering. SAUL1 and AtPUB43 
      could produce tethering in uninfected tissue when paired with MVB-binding 
      proteins or when their E3 ligase domain was deleted. When Nicotiana benthamiana 
      leaf tissue was infected with Phytophthora capsici, full length SAUL1 and AtPUB43 
      localized in membrane patches consistent with PM-MVB/TP tethering. Our findings 
      define new tools for studying PM-MVB/TP tethering and its possible role in plant 
      defense. SIGNIFICANCE STATEMENT: Although not previously observed, the tethering 
      of multi-vesicular bodies to the plasma membrane is of interest due to the 
      potential role of this process in producing exosomes in plants. Here we describe 
      tools for observing and manipulating the tethering of multi-vesicular bodies and 
      the tonoplast to the plant plasma membrane, and describe two plant proteins that 
      may naturally regulate this process during infection.
FAU - Tao, Kai
AU  - Tao K
AD  - Molecular and Cellular Biology Program, Oregon State University, Corvallis, OR, 
      United States.
AD  - Department of Botany and Plant Pathology, Oregon State University, Corvallis, OR, 
      United States.
FAU - Waletich, Justin R
AU  - Waletich JR
AD  - Department of Botany and Plant Pathology, Oregon State University, Corvallis, OR, 
      United States.
FAU - Wise, Hua
AU  - Wise H
AD  - Department of Botany and Plant Pathology, Oregon State University, Corvallis, OR, 
      United States.
FAU - Arredondo, Felipe
AU  - Arredondo F
AD  - Department of Botany and Plant Pathology, Oregon State University, Corvallis, OR, 
      United States.
FAU - Tyler, Brett M
AU  - Tyler BM
AD  - Molecular and Cellular Biology Program, Oregon State University, Corvallis, OR, 
      United States.
AD  - Department of Botany and Plant Pathology, Oregon State University, Corvallis, OR, 
      United States.
AD  - Center for Genome Research and Biocomputing, Oregon State University, Corvallis, 
      OR, United States.
LA  - eng
PT  - Journal Article
DEP - 20190522
PL  - Switzerland
TA  - Front Plant Sci
JT  - Frontiers in plant science
JID - 101568200
PMC - PMC6662526
OTO - NOTNLM
OT  - BiFC
OT  - multi-vesicular bodies
OT  - plasma membrane
OT  - tethering
OT  - tonoplast
EDAT- 2019/08/10 06:00
MHDA- 2019/08/10 06:01
PMCR- 2019/01/01
CRDT- 2019/08/10 06:00
PHST- 2019/01/16 00:00 [received]
PHST- 2019/04/26 00:00 [accepted]
PHST- 2019/08/10 06:00 [entrez]
PHST- 2019/08/10 06:00 [pubmed]
PHST- 2019/08/10 06:01 [medline]
PHST- 2019/01/01 00:00 [pmc-release]
AID - 10.3389/fpls.2019.00636 [doi]
PST - epublish
SO  - Front Plant Sci. 2019 May 22;10:636. doi: 10.3389/fpls.2019.00636. eCollection 
      2019.