Plasma membrane phospholipid signature recruits the plant exocyst complex via the EXO70A1 subunit

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61389030%3A_____%2F21%3A00551596" target="_blank" >RIV/61389030:_____/21:00551596 - isvavai.cz</a>

Alternative codes found

RIV/60461373:22330/21:43922725

Result on the web

<a href="http://doi.org/10.1073/pnas.2105287118" target="_blank" >http://doi.org/10.1073/pnas.2105287118</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1073/pnas.2105287118" target="_blank" >10.1073/pnas.2105287118</a>

Result language

angličtina

Original language name

Plasma membrane phospholipid signature recruits the plant exocyst complex via the EXO70A1 subunit

Original language description

Polarized exocytosis is essential for many vital processes in eukaryotic cells, where secretory vesicles are targeted to distinct plasma membrane domains characterized by their specific lipid-protein composition. Heterooctameric protein complex exocyst facilitates the vesicle tethering to a target membrane and is a principal cell polarity regulator in eukaryotes. The architecture and molecular details of plant exocyst and its membrane recruitment have remained elusive. Here, we show that the plant exocyst consists of two modules formed by SEC3-SEC5-SEC6-SEC8 and SEC10-SEC15-EXO70- EXO84 subunits, respectively, documenting the evolutionarily conserved architecture within eukaryotes. In contrast to yeast and mammals, the two modules are linked by a plant-specific SEC3- EXO70 interaction, and plant EXO70 functionally dominates over SEC3 in the exocyst recruitment to the plasma membrane. Using an interdisciplinary approach, we found that the C-terminal part of EXO70A1, the canonical EXO70 isoform in Arabidopsis, is critical for this process. In contrast to yeast and animal cells, the EXO70A1 interaction with the plasma membrane is mediated by multiple anionic phospholipids uniquely contributing to the plant plasma membrane identity. We identified several evolutionary conserved EXO70 lysine residues and experimentally proved their importance for the EXO70A1-phospholipid interactions. Collectively, our work has uncovered plant-specific features of the exocyst complex and emphasized the importance of the specific protein-lipid code for the recruitment of peripheral membrane proteins.

Czech name

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Czech description

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Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

—

OECD FORD branch

10601 - Cell biology

Project

Result was created during the realization of more than one project. More information in the Projects tab.

Continuities

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year

2021

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

Proceedings of the National Academy of Sciences of the United States of America

ISSN

0027-8424

e-ISSN

—

Volume of the periodical

118

Issue of the periodical within the volume

36

Country of publishing house

US - UNITED STATES

Number of pages

12

Pages from-to

e2105287118

UT code for WoS article

000694705600001

EID of the result in the Scopus database

2-s2.0-85114132837