The PIN-FORMED (PIN) protein family of auxin transporters

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61389030%3A_____%2F09%3A00336003" target="_blank" >RIV/61389030:_____/09:00336003 - isvavai.cz</a>

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

The PIN-FORMED (PIN) protein family of auxin transporters

Popis výsledku v původním jazyce

The PIN-FORMED (PIN) proteins are secondary transporters acting predominantly in the efflux of the plant signal molecule auxin from cells. They are asymmetrically localized within cells and their polarity determines the directionality of intercellular auxin flow. PIN genes are found exclusively in the genomes of multicellular plants and they encode proteins that play an important role in regulating asymmetric auxin distribution in multiple developmental processes. All PIN proteins have similar structurewith amino- and carboxy-terminal hydrophobic, membrane-spanning domains separated by a central hydrophilic domain. PIN proteins possessing the large hydrophilic domain localize to plasma membrane. In contrast, those PINs having this domain reduced or lacking localize to endoplasmic reticulum; they regulate subcellular compartmentalization of auxin and thus the auxin metabolism. The activity of PIN proteins is regulated at multiple levels including environmental signals.

Název v anglickém jazyce

The PIN-FORMED (PIN) protein family of auxin transporters

Popis výsledku anglicky

The PIN-FORMED (PIN) proteins are secondary transporters acting predominantly in the efflux of the plant signal molecule auxin from cells. They are asymmetrically localized within cells and their polarity determines the directionality of intercellular auxin flow. PIN genes are found exclusively in the genomes of multicellular plants and they encode proteins that play an important role in regulating asymmetric auxin distribution in multiple developmental processes. All PIN proteins have similar structurewith amino- and carboxy-terminal hydrophobic, membrane-spanning domains separated by a central hydrophilic domain. PIN proteins possessing the large hydrophilic domain localize to plasma membrane. In contrast, those PINs having this domain reduced or lacking localize to endoplasmic reticulum; they regulate subcellular compartmentalization of auxin and thus the auxin metabolism. The activity of PIN proteins is regulated at multiple levels including environmental signals.

Druh

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

CEP obor

EB - Genetika a molekulární biologie

OECD FORD obor

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Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2009

Kód důvěrnosti údajů

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

Název periodika

Genome Biology

ISSN

1474-760X

e-ISSN

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Svazek periodika

10

Číslo periodika v rámci svazku

12

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

11

Strana od-do

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Kód UT WoS článku

000274289000004

EID výsledku v databázi Scopus

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