N-terminus of seed caleosins is essential for lipid droplet sorting but not for lipid accumulation

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60461373%3A22330%2F15%3A43899753" target="_blank" >RIV/60461373:22330/15:43899753 - isvavai.cz</a>

Výsledek na webu

<a href="http://www.sciencedirect.com/science/article/pii/S0003986115002544" target="_blank" >http://www.sciencedirect.com/science/article/pii/S0003986115002544</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.abb.2015.05.008" target="_blank" >10.1016/j.abb.2015.05.008</a>

Jazyk výsledku

angličtina

Název v původním jazyce

N-terminus of seed caleosins is essential for lipid droplet sorting but not for lipid accumulation

Popis výsledku v původním jazyce

Caleosin, a calcium-binding protein associated with plant lipid droplets, stimulates lipid accumulation when heterologously expressed in Saccharomyces cerevisiae. Accumulated lipids are stored in cytoplasmic lipid droplets that are stabilised by incorporated caleosin. We designed a set of mutants affecting putative crucial sites for caleosin function and association with lipid droplets, i.e. the N-terminus, the EF-hand motif and the proline-knot motif. We investigated the effect of introduced mutationson caleosin capacity to initiate lipid accumulation and on caleosin sorting within cell as well as on its association with lipid droplets. Our results strongly suggest that the N-terminal domain is essential for proper protein sorting and targeting to lipid droplets but not for enhancing lipid accumulation.

Název v anglickém jazyce

N-terminus of seed caleosins is essential for lipid droplet sorting but not for lipid accumulation

Popis výsledku anglicky

Caleosin, a calcium-binding protein associated with plant lipid droplets, stimulates lipid accumulation when heterologously expressed in Saccharomyces cerevisiae. Accumulated lipids are stored in cytoplasmic lipid droplets that are stabilised by incorporated caleosin. We designed a set of mutants affecting putative crucial sites for caleosin function and association with lipid droplets, i.e. the N-terminus, the EF-hand motif and the proline-knot motif. We investigated the effect of introduced mutationson caleosin capacity to initiate lipid accumulation and on caleosin sorting within cell as well as on its association with lipid droplets. Our results strongly suggest that the N-terminal domain is essential for proper protein sorting and targeting to lipid droplets but not for enhancing lipid accumulation.

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

—

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2015

Kód důvěrnosti údajů

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

Název periodika

Archives of Biochemistry and Biophysics

ISSN

0003-9861

e-ISSN

—

Svazek periodika

579

Číslo periodika v rámci svazku

1.8.2015

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

8

Strana od-do

47-54

Kód UT WoS článku

000358552000007

EID výsledku v databázi Scopus

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