How alternative splicing changes the properties of plant proteins

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61389030%3A_____%2F22%3A00565617" target="_blank" >RIV/61389030:_____/22:00565617 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/00216224:14310/22:00135036

Výsledek na webu

<a href="https://doi.org/10.1017/qpb.2022.9" target="_blank" >https://doi.org/10.1017/qpb.2022.9</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1017/qpb.2022.9" target="_blank" >10.1017/qpb.2022.9</a>

Jazyk výsledku

angličtina

Název v původním jazyce

How alternative splicing changes the properties of plant proteins

Popis výsledku v původním jazyce

Most plant primary transcripts undergo alternative splicing (AS), and its impact on protein diversity is a subject of intensive investigation. Several studies have uncovered various mechanisms of how particular protein splice isoforms operate. However, the common principles behind the AS effects on protein function in plants have rarely been surveyed. Here, on the selected examples, we highlight diverse tissue expression patterns, subcellular localization, enzymatic activities, abilities to bind other molecules and other relevant features. We describe how the protein isoforms mutually interact to underline their intriguing roles in altering the functionality of protein complexes. Moreover, we also discuss the known cases when these interactions have been placed inside the autoregulatory loops. This review is particularly intended for plant cell and developmental biologists who would like to gain inspiration on how the splice variants encoded by their genes of interest may coordinately work.

Název v anglickém jazyce

How alternative splicing changes the properties of plant proteins

Popis výsledku anglicky

Most plant primary transcripts undergo alternative splicing (AS), and its impact on protein diversity is a subject of intensive investigation. Several studies have uncovered various mechanisms of how particular protein splice isoforms operate. However, the common principles behind the AS effects on protein function in plants have rarely been surveyed. Here, on the selected examples, we highlight diverse tissue expression patterns, subcellular localization, enzymatic activities, abilities to bind other molecules and other relevant features. We describe how the protein isoforms mutually interact to underline their intriguing roles in altering the functionality of protein complexes. Moreover, we also discuss the known cases when these interactions have been placed inside the autoregulatory loops. This review is particularly intended for plant cell and developmental biologists who would like to gain inspiration on how the splice variants encoded by their genes of interest may coordinately work.

Druh

J_SC - Článek v periodiku v databázi SCOPUS

CEP obor

—

OECD FORD obor

10609 - Biochemical research methods

Projekt

<a href="/cs/project/EF16_019%2F0000738" target="_blank" >EF16_019/0000738: Centrum experimentální biologie rostlin</a><br>

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2022

Kód důvěrnosti údajů

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

Název periodika

Quantitative Plant Biology

ISSN

2632-8828

e-ISSN

2632-8828

Svazek periodika

3

Číslo periodika v rámci svazku

Jul

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

11

Strana od-do

e14

Kód UT WoS článku

—

EID výsledku v databázi Scopus

2-s2.0-85146657247