Fatty acid modification of Wnt1 and Wnt3a at serine is
prerequisite for lipidation at cysteine and is essential for
Wnt signalling

J 2011

Fatty acid modification of Wnt1 and Wnt3a at serine is prerequisite for lipidation at cysteine and is essential for Wnt signalling

DOUBRAVSKA, L; M KRAUSOVA; D GRADL; M VOJTECHOVA; L TUMOVA et al.

Základní údaje

Originální název

Fatty acid modification of Wnt1 and Wnt3a at serine is prerequisite for lipidation at cysteine and is essential for Wnt signalling

Autoři

DOUBRAVSKA, L; M KRAUSOVA; D GRADL; M VOJTECHOVA; L TUMOVA; J LUKAS; T VALENTA; Vendula POSPÍCHALOVÁ; Bohumil FAFÍLEK; J PLACHY; O SEBESTA a V KORINEK

Vydání

Cellular Signalling, NEW YORK, ELSEVIER SCIENCE INC, 2011, 0898-6568

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Utajení

není předmětem státního či obchodního tajemství

Impakt faktor

Impact factor: 4.058

Označené pro přenos do RIV

DOI

https://doi.org/10.1016/j.cellsig.2011.01.007

UT WoS

000288977400011

Klíčová slova anglicky

Wnt signalling; Post-translational modification; Acylation; N-glycosylation; Double axis formation; TCF/beta-catenin transcription

Změněno: 3. 11. 2015 22:52, RNDr. Vendula Hlaváčková Pospíchalová, Ph.D.

Anotace

V originále

The Wnt family of proteins is a group of extracellular signalling molecules that regulate cell-fate decisions in developing and adult tissues. It is presumed that all 19 mammalian Wnt family members contain two types of post-translational modification: the covalent attachment of fatty acids at two distinct positions, and the N-glycosylation of multiple asparagines. We examined how these modifications contribute to the secretion, extracellular movement and signalling activity of mouse Wnt1 and Wnt3a ligands. We revealed that O-linked acylation of serine is required for the subsequent S-palmitoylation of cysteine. As such, mutant proteins that lack the crucial serine residue are not lipidated. Interestingly, although double-acylation of Wnt1 was indispensable for signalling in mammalian cells, in Xenopus embryos the S-palmitoyl-deficient form retained the signalling activity. In the case of Wnt3a, the functional duality of the attached acyls was less prominent, since the ligand lacking S-linked palmitate was still capable of signalling in various cellular contexts. Finally, we show that the signalling competency of both Wnt1 and Wnt3a is related to their ability to associate with the extracellular matrix. (C) 2011 Elsevier Inc. All rights reserved.

Citovat

DOUBRAVSKA, L; M KRAUSOVA; D GRADL; M VOJTECHOVA; L TUMOVA; J LUKAS; T VALENTA; Vendula POSPÍCHALOVÁ; Bohumil FAFÍLEK; J PLACHY; O SEBESTA a V KORINEK. Fatty acid modification of Wnt1 and Wnt3a at serine is prerequisite for lipidation at cysteine and is essential for Wnt signalling. Cellular Signalling. NEW YORK: ELSEVIER SCIENCE INC, 2011, roč. 23, č. 5, s. 837-848. ISSN 0898-6568. Dostupné z: https://doi.org/10.1016/j.cellsig.2011.01.007.

@article{1316070,
   author = {Doubravska, L and Krausova, M and Gradl, D and Vojtechova, M and Tumova, L and Lukas, J and Valenta, T and Pospíchalová, Vendula and Fafílek, Bohumil and Plachy, J and Sebesta, O and Korinek, V},
   article_location = {NEW YORK},
   article_number = {5},
   doi = {https://doi.org/10.1016/j.cellsig.2011.01.007},
   keywords = {Wnt signalling; Post-translational modification; Acylation; N-glycosylation; Double axis formation; TCF/beta-catenin transcription},
   language = {eng},
   issn = {0898-6568},
   journal = {Cellular Signalling},
   title = {Fatty acid modification of Wnt1 and Wnt3a at serine is prerequisite for lipidation at cysteine and is essential for Wnt signalling},
   volume = {23},
   year = {2011}
}

TY  - JOUR
ID  - 1316070
AU  - Doubravska, L - Krausova, M - Gradl, D - Vojtechova, M - Tumova, L - Lukas, J - Valenta, T - Pospíchalová, Vendula - Fafílek, Bohumil - Plachy, J - Sebesta, O - Korinek, V
PY  - 2011
TI  - Fatty acid modification of Wnt1 and Wnt3a at serine is prerequisite for lipidation at cysteine and is essential for Wnt signalling
JF  - Cellular Signalling
VL  - 23
IS  - 5
SP  - 837-848
EP  - 837-848
PB  - ELSEVIER SCIENCE INC
SN  - 08986568
KW  - Wnt signalling
KW  - Post-translational modification
KW  - Acylation
KW  - N-glycosylation
KW  - Double axis formation
KW  - TCF/beta-catenin transcription
N2  - The Wnt family of proteins is a group of extracellular signalling molecules that regulate cell-fate decisions in developing and adult tissues. It is presumed that all 19 mammalian Wnt family members contain two types of post-translational modification: the covalent attachment of fatty acids at two distinct positions, and the N-glycosylation of multiple asparagines. We examined how these modifications contribute to the secretion, extracellular movement and signalling activity of mouse Wnt1 and Wnt3a ligands. We revealed that O-linked acylation of serine is required for the subsequent S-palmitoylation of cysteine. As such, mutant proteins that lack the crucial serine residue are not lipidated. Interestingly, although double-acylation of Wnt1 was indispensable for signalling in mammalian cells, in Xenopus embryos the S-palmitoyl-deficient form retained the signalling activity. In the case of Wnt3a, the functional duality of the attached acyls was less prominent, since the ligand lacking S-linked palmitate was still capable of signalling in various cellular contexts. Finally, we show that the signalling competency of both Wnt1 and Wnt3a is related to their ability to associate with the extracellular matrix. (C) 2011 Elsevier Inc. All rights reserved.
ER  -

DOUBRAVSKA, L; M KRAUSOVA; D GRADL; M VOJTECHOVA; L TUMOVA; J LUKAS; T VALENTA; Vendula POSPÍCHALOVÁ; Bohumil FAFÍLEK; J PLACHY; O SEBESTA a V KORINEK. Fatty acid modification of Wnt1 and Wnt3a at serine is prerequisite for lipidation at cysteine and is essential for Wnt signalling. \textit{Cellular Signalling}. NEW YORK: ELSEVIER SCIENCE INC, 2011, roč.~23, č.~5, s.~837-848. ISSN~0898-6568. Dostupné z: https://doi.org/10.1016/j.cellsig.2011.01.007.

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