Phosphorylation of HORMA-domain protein HTP-3 at Serine 285 is
dispensable for crossover formation

J 2022

Phosphorylation of HORMA-domain protein HTP-3 at Serine 285 is dispensable for crossover formation

DAS, Debabrata, Shalini TRIVEDI, Jitka BLAŽÍČKOVÁ, Swathi ARUR, Nicola SILVA et. al.

Základní údaje

Originální název

Phosphorylation of HORMA-domain protein HTP-3 at Serine 285 is dispensable for crossover formation

Autoři

DAS, Debabrata, Shalini TRIVEDI (356 Indie, domácí), Jitka BLAŽÍČKOVÁ (203 Česká republika, domácí), Swathi ARUR a Nicola SILVA (380 Itálie, garant, domácí)

Vydání

G3-Genes, Genomes, Genetics, CARY, OXFORD UNIV PRESS INC, 2022, 2160-1836

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10603 Genetics and heredity

Stát vydavatele

Spojené státy

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 2.600

Kód RIV

RIV/00216224:14110/22:00128180

Organizační jednotka

Lékařská fakulta

DOI

http://dx.doi.org/10.1093/g3journal/jkac079

UT WoS

000786255000001

Klíčová slova anglicky

Caenorhabditis elegans meiosis; HORMA-domain proteins; HTP-3

Štítky

14110513, CF CELLIM, rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 28. 8. 2024 10:25, Mgr. Michal Petr

Anotace

V originále

Generation of functional gametes is accomplished through a multilayered and finely orchestrated succession of events during meiotic progression. In the Caenorhabditis elegans germline, the HORMA-domain-containing protein HTP-3 plays pivotal roles for the establishment of chromosome axes and the efficient induction of programmed DNA double-strand breaks, both of which are crucial for crossover formation. Double-strand breaks allow for accurate chromosome segregation during the first meiotic division and therefore are an essential requirement for the production of healthy gametes. Phosphorylation-dependent regulation of HORMAD protein plays important roles in controlling meiotic chromosome behavior. Here, we document a phospho-site in HTP-3 at Serine 285 that is constitutively phosphorylated during meiotic prophase I. pHTP-3(S285) localization overlaps with panHTP-3 except in nuclei undergoing physiological apoptosis, in which pHTP-3 is absent. Surprisingly, we observed that phosphorylation of HTP-3 at S285 is independent of the canonical kinases that control meiotic progression in nematodes. During meiosis, the htp-3(S285A) mutant displays accelerated RAD-51 turnover, but no other meiotic abnormalities. Altogether, these data indicate that the Ser285 phosphorylation is independent of canonical meiotic protein kinases and does not regulate HTP-3-dependent meiotic processes. We propose a model wherein phosphorylation of HTP-3 occurs through noncanonical or redundant meiotic kinases and/or is likely redundant with additional phospho-sites for function in vivo.

Návaznosti

GA20-08819S, projekt VaV

Název: Pochopení úlohy PARG při podpoře tvorby a oprav dvouřetězcových zlomů DNA v meióze

Investor: Grantová agentura ČR, Pochopení úlohy PARG při podpoře tvorby a oprav dvouřetězcových zlomů DNA v meióze

LM2018129, projekt VaV

Název: Národní infrastruktura pro biologické a medicínské zobrazování Czech-BioImaging

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, National research infrastructure for biological and medical imaging

MUNI/A/1418/2021, interní kód MU

Název: Biomedicínské vědy II (Akronym: BIOMED)

Investor: Masarykova univerzita, Biomedicínské vědy II

Citovat

DAS, Debabrata, Shalini TRIVEDI, Jitka BLAŽÍČKOVÁ, Swathi ARUR a Nicola SILVA. Phosphorylation of HORMA-domain protein HTP-3 at Serine 285 is dispensable for crossover formation. G3-Genes, Genomes, Genetics. CARY: OXFORD UNIV PRESS INC, 2022, roč. 12, č. 5, s. 1-10. ISSN 2160-1836. Dostupné z: https://dx.doi.org/10.1093/g3journal/jkac079.

@article{2248093,
   author = {Das, Debabrata and Trivedi, Shalini and Blažíčková, Jitka and Arur, Swathi and Silva, Nicola},
   article_location = {CARY},
   article_number = {5},
   doi = {http://dx.doi.org/10.1093/g3journal/jkac079},
   keywords = {Caenorhabditis elegans meiosis; HORMA-domain proteins; HTP-3},
   language = {eng},
   issn = {2160-1836},
   journal = {G3-Genes, Genomes, Genetics},
   title = {Phosphorylation of HORMA-domain protein HTP-3 at Serine 285 is dispensable for crossover formation},
   url = {https://academic.oup.com/g3journal/article/12/5/jkac079/6564663?login=true},
   volume = {12},
   year = {2022}
}

TY  - JOUR
ID  - 2248093
AU  - Das, Debabrata - Trivedi, Shalini - Blažíčková, Jitka - Arur, Swathi - Silva, Nicola
PY  - 2022
TI  - Phosphorylation of HORMA-domain protein HTP-3 at Serine 285 is dispensable for crossover formation
JF  - G3-Genes, Genomes, Genetics
VL  - 12
IS  - 5
SP  - 1-10
EP  - 1-10
PB  - OXFORD UNIV PRESS INC
SN  - 21601836
KW  - Caenorhabditis elegans meiosis
KW  - HORMA-domain proteins
KW  - HTP-3
UR  - https://academic.oup.com/g3journal/article/12/5/jkac079/6564663?login=true
N2  - Generation of functional gametes is accomplished through a multilayered and finely orchestrated succession of events during meiotic progression. In the Caenorhabditis elegans germline, the HORMA-domain-containing protein HTP-3 plays pivotal roles for the establishment of chromosome axes and the efficient induction of programmed DNA double-strand breaks, both of which are crucial for crossover formation. Double-strand breaks allow for accurate chromosome segregation during the first meiotic division and therefore are an essential requirement for the production of healthy gametes. Phosphorylation-dependent regulation of HORMAD protein plays important roles in controlling meiotic chromosome behavior. Here, we document a phospho-site in HTP-3 at Serine 285 that is constitutively phosphorylated during meiotic prophase I. pHTP-3(S285) localization overlaps with panHTP-3 except in nuclei undergoing physiological apoptosis, in which pHTP-3 is absent. Surprisingly, we observed that phosphorylation of HTP-3 at S285 is independent of the canonical kinases that control meiotic progression in nematodes. During meiosis, the htp-3(S285A) mutant displays accelerated RAD-51 turnover, but no other meiotic abnormalities. Altogether, these data indicate that the Ser285 phosphorylation is independent of canonical meiotic protein kinases and does not regulate HTP-3-dependent meiotic processes. We propose a model wherein phosphorylation of HTP-3 occurs through noncanonical or redundant meiotic kinases and/or is likely redundant with additional phospho-sites for function in vivo.
ER  -

DAS, Debabrata, Shalini TRIVEDI, Jitka BLAŽÍČKOVÁ, Swathi ARUR a Nicola SILVA. Phosphorylation of HORMA-domain protein HTP-3 at Serine 285 is dispensable for crossover formation. \textit{G3-Genes, Genomes, Genetics}. CARY: OXFORD UNIV PRESS INC, 2022, roč.~12, č.~5, s.~1-10. ISSN~2160-1836. Dostupné z: https://dx.doi.org/10.1093/g3journal/jkac079.

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