GpsB Coordinates StkP Signaling as a PASTA Kinase Adaptor in
Streptococcus pneumoniae Cell Division

J 2024

GpsB Coordinates StkP Signaling as a PASTA Kinase Adaptor in Streptococcus pneumoniae Cell Division

STAUBEROVA, Vaclava; Bohumil KUBESA; Merrin JOSEPH; Mattia BENEDET; Berenice FURLAN et al.

Základní údaje

Originální název

GpsB Coordinates StkP Signaling as a PASTA Kinase Adaptor in Streptococcus pneumoniae Cell Division

Autoři

Vydání

Journal of Molecular Biology, LONDON, ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD, 2024, 0022-2836

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10608 Biochemistry and molecular biology

Stát vydavatele

Velká Británie a Severní Irsko

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 4.500

Označené pro přenos do RIV

Ano

Kód RIV

RIV/00216224:90242/24:00139177

Organizační jednotka

CIISB III

Klíčová slova anglicky

cell signalling; Ser/Thr protein kinase; phosphorylation; cell division; protein-protein interaction

Štítky

ne MU, rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 26. 3. 2025 21:28, Mgr. Eva Dubská

Anotace

V originále

StkP, the Ser/Thr protein kinase of the major human pathogen Streptococcus pneumoniae, , monitors cell wall signals and regulates growth and division in response. In vivo, , StkP interacts with GpsB, a cell division protein required for septal ring formation and closure, that affects StkP-dependent phosphorylation. Here, we report that although StkP has basal intrinsic kinase activity, GpsB promotes efficient autophosphorylation of StkP and phosphorylation of StkP substrates. Phosphoproteomic analyzes showed that GpsB is phosphorylated at several Ser and Thr residues. We confirmed that StkP directly phosphorylates GpsB in vitro and in vivo, , with T79 and T83 being the major phosphorylation sites. In vitro, , phosphoablative GpsB substitutions had a lower potential to stimulate StkP activity, whereas phosphomimetic substitutions were functional in terms of StkP activation. In vivo, , substitutions of GpsB phosphoacceptor residues, either phosphoablative or mimetic, had a negative effect on GpsB function, resulting in reduced StkP-dependent phosphorylation and impaired cell division. The bacterial two-hybrid assay and coimmunoprecipitation of GpsB from cells with differentially active StkP indicated that increased phosphorylation of GpsB resulted in a more efficient interaction of GpsB with StkP. Our data suggest that GpsB acts as an adaptor that directly promotes StkP activity by mediating interactions within the StkP signaling hub, ensuring StkP recruitment into the complex and substrate specificity. We present a model that interaction of StkP with GpsB and its phosphorylation and dephosphorylation dynamically modulate kinase activity during exponential growth and under cell wall stress of S. pneumoniae, , ensuring the proper functioning of the StkP signaling pathway. (c) 2024 The Author(s). Published by Elsevier Ltd.

Návaznosti

90242, velká výzkumná infrastruktura

Název: CIISB III

Citovat

STAUBEROVA, Vaclava; Bohumil KUBESA; Merrin JOSEPH; Mattia BENEDET; Berenice FURLAN; Karolina BURIANKOVA; Ales ULRYCH; Rudolf KUPCIK; Tomas VOMASTEK; Orietta MASSIDDA; Ho-Ching T TSUI; Malcolm E WINKLER; Pavel BRANNY a Linda DOUBRAVOVA. GpsB Coordinates StkP Signaling as a PASTA Kinase Adaptor in Streptococcus pneumoniae Cell Division. Journal of Molecular Biology. LONDON: ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD, 2024, roč. 436, č. 22, s. 1-24. ISSN 0022-2836. Dostupné z: https://doi.org/10.1016/j.jmb.2024.168797.

@article{2486899,
 author = {Stauberova, Vaclava and Kubesa, Bohumil and Joseph, Merrin and Benedet, Mattia and Furlan, Berenice and Buriankova, Karolina and Ulrych, Ales and Kupcik, Rudolf and Vomastek, Tomas and Massidda, Orietta and Tsui, HoandChing T and Winkler, Malcolm E and Branny, Pavel and Doubravova, Linda},
 article_location = {LONDON},
 article_number = {22},
 doi = {https://doi.org/10.1016/j.jmb.2024.168797},
 keywords = {cell signalling; Ser/Thr protein kinase; phosphorylation; cell division; protein-protein interaction},
 language = {eng},
 issn = {0022-2836},
 journal = {Journal of Molecular Biology},
 title = {GpsB Coordinates StkP Signaling as a PASTA Kinase Adaptor in Streptococcus pneumoniae Cell Division},
 url = {https://www.sciencedirect.com/science/article/pii/S0022283624004194?via%3Dihub},
 volume = {436},
 year = {2024}
}

TY - JOUR
ID - 2486899
AU - Stauberova, Vaclava - Kubesa, Bohumil - Joseph, Merrin - Benedet, Mattia - Furlan, Berenice - Buriankova, Karolina - Ulrych, Ales - Kupcik, Rudolf - Vomastek, Tomas - Massidda, Orietta - Tsui, Ho-Ching T - Winkler, Malcolm E - Branny, Pavel - Doubravova, Linda
PY - 2024
TI - GpsB Coordinates StkP Signaling as a PASTA Kinase Adaptor in Streptococcus pneumoniae Cell Division
JF - Journal of Molecular Biology
VL - 436
IS - 22
SP - 1-24
EP - 1-24
PB - ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
SN - 00222836
KW - cell signalling
KW - Ser/Thr protein kinase
KW - phosphorylation
KW - cell division
KW - protein-protein interaction
UR - https://www.sciencedirect.com/science/article/pii/S0022283624004194?via%3Dihub
N2 - StkP, the Ser/Thr protein kinase of the major human pathogen Streptococcus pneumoniae, , monitors cell wall signals and regulates growth and division in response. In vivo, , StkP interacts with GpsB, a cell division protein required for septal ring formation and closure, that affects StkP-dependent phosphorylation. Here, we report that although StkP has basal intrinsic kinase activity, GpsB promotes efficient autophosphorylation of StkP and phosphorylation of StkP substrates. Phosphoproteomic analyzes showed that GpsB is phosphorylated at several Ser and Thr residues. We confirmed that StkP directly phosphorylates GpsB in vitro and in vivo, , with T79 and T83 being the major phosphorylation sites. In vitro, , phosphoablative GpsB substitutions had a lower potential to stimulate StkP activity, whereas phosphomimetic substitutions were functional in terms of StkP activation. In vivo, , substitutions of GpsB phosphoacceptor residues, either phosphoablative or mimetic, had a negative effect on GpsB function, resulting in reduced StkP-dependent phosphorylation and impaired cell division. The bacterial two-hybrid assay and coimmunoprecipitation of GpsB from cells with differentially active StkP indicated that increased phosphorylation of GpsB resulted in a more efficient interaction of GpsB with StkP. Our data suggest that GpsB acts as an adaptor that directly promotes StkP activity by mediating interactions within the StkP signaling hub, ensuring StkP recruitment into the complex and substrate specificity. We present a model that interaction of StkP with GpsB and its phosphorylation and dephosphorylation dynamically modulate kinase activity during exponential growth and under cell wall stress of S. pneumoniae, , ensuring the proper functioning of the StkP signaling pathway. (c) 2024 The Author(s). Published by Elsevier Ltd.
ER -

STAUBEROVA, Vaclava; Bohumil KUBESA; Merrin JOSEPH; Mattia BENEDET; Berenice FURLAN; Karolina BURIANKOVA; Ales ULRYCH; Rudolf KUPCIK; Tomas VOMASTEK; Orietta MASSIDDA; Ho-Ching T TSUI; Malcolm E WINKLER; Pavel BRANNY a Linda DOUBRAVOVA. GpsB Coordinates StkP Signaling as a PASTA Kinase Adaptor in\&{}lt;i\&{}gt; Streptococcus\&{}lt;/i\&{}gt;\&{}lt;i\&{}gt; pneumoniae\&{}lt;/i\&{}gt; Cell Division. \textit{Journal of Molecular Biology}. LONDON: ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD, 2024, roč.~436, č.~22, s.~1-24. ISSN~0022-2836. Dostupné z: https://doi.org/10.1016/j.jmb.2024.168797.

Přehled o publikaci

GpsB Coordinates StkP Signaling as a PASTA Kinase Adaptor in<i> Streptococcus</i><i> pneumoniae</i> Cell Division