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Article ; Online: Pathogen-specific structural features of

Manso, José A / Carabias, Arturo / Sárkány, Zsuzsa / de Pereda, José M / Pereira, Pedro José Barbosa / Macedo-Ribeiro, Sandra

mBio

2023 Volume 14, Issue 4, Page(s) e0063823

Abstract: An important feature associated ... ...

Abstract	An important feature associated with
MeSH term(s)	Humans ; Candida albicans ; Antifungal Agents/pharmacology ; Antifungal Agents/metabolism ; Candidiasis/microbiology ; Signal Transduction ; Guanine Nucleotide Exchange Factors/metabolism ; Fungal Proteins/genetics ; Fungal Proteins/metabolism ; Hyphae
Chemical Substances	Antifungal Agents ; Guanine Nucleotide Exchange Factors ; Fungal Proteins
Language	English
Publishing date	2023-08-01
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2557172-2
ISSN	2150-7511 ; 2161-2129
ISSN (online)	2150-7511
ISSN	2161-2129
DOI	10.1128/mbio.00638-23
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Article: C3G self-regulatory mechanism revealed: implications for hematopoietic malignancies.

Carabias, Arturo / Guerrero, Carmen / de Pereda, José M

Molecular & cellular oncology

2020 Volume 8, Issue 1, Page(s) 1837581

Abstract: Abnormally increased signaling by the GTPase RAP1 favors progression of diverse tumors. We have characterized the auto-regulation and activation of C3G (RAPGEF1), an activator of RAP1. This led us to discover mutations in non-Hodgkin's lymphomas that ... ...

Abstract	Abnormally increased signaling by the GTPase RAP1 favors progression of diverse tumors. We have characterized the auto-regulation and activation of C3G (RAPGEF1), an activator of RAP1. This led us to discover mutations in non-Hodgkin's lymphomas that activate C3G-RAP1 constitutively, suggesting that deregulation of C3G may favor the dissemination of tumor cells.
Language	English
Publishing date	2020-12-01
Publishing country	United States
Document type	Journal Article
ISSN	2372-3556
ISSN	2372-3556
DOI	10.1080/23723556.2020.1837581
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Article ; Online: Regulation of hemidesmosome dynamics and cell signaling by integrin α6β4.

Te Molder, Lisa / de Pereda, Jose M / Sonnenberg, Arnoud

Journal of cell science

2021 Volume 134, Issue 18

Abstract: Hemidesmosomes (HDs) are specialized multiprotein complexes that connect the keratin cytoskeleton of epithelial cells to the extracellular matrix (ECM). In the skin, these complexes provide stable adhesion of basal keratinocytes to the underlying ... ...

Abstract	Hemidesmosomes (HDs) are specialized multiprotein complexes that connect the keratin cytoskeleton of epithelial cells to the extracellular matrix (ECM). In the skin, these complexes provide stable adhesion of basal keratinocytes to the underlying basement membrane. Integrin α6β4 is a receptor for laminins and plays a vital role in mediating cell adhesion by initiating the assembly of HDs. In addition, α6β4 has been implicated in signal transduction events that regulate diverse cellular processes, including proliferation and survival. In this Review, we detail the role of α6β4 in HD assembly and beyond, and we discuss the molecular mechanisms that regulate its function.
MeSH term(s)	Cell Adhesion ; Hemidesmosomes ; Integrin alpha6beta4/genetics ; Keratinocytes ; Signal Transduction
Chemical Substances	Integrin alpha6beta4
Language	English
Publishing date	2021-09-15
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2993-2
ISSN	1477-9137 ; 0021-9533
ISSN (online)	1477-9137
ISSN	0021-9533
DOI	10.1242/jcs.259004
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Zs.A 1200: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
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Article ; Online: Crk proteins activate the Rap1 guanine nucleotide exchange factor C3G by segregated adaptor-dependent and -independent mechanisms.

Rodríguez-Blázquez, Antonio / Carabias, Arturo / Morán-Vaquero, Alba / de Cima, Sergio / Luque-Ortega, Juan R / Alfonso, Carlos / Schuck, Peter / Manso, José Antonio / Macedo-Ribeiro, Sandra / Guerrero, Carmen / de Pereda, José M

Cell communication and signaling : CCS

2023 Volume 21, Issue 1, Page(s) 30

Abstract: Background: C3G is a guanine nucleotide exchange factor (GEF) that activates Rap1 to promote cell adhesion. Resting C3G is autoinhibited and the GEF activity is released by stimuli that signal through tyrosine kinases. C3G is activated by tyrosine ... ...

Abstract	Background: C3G is a guanine nucleotide exchange factor (GEF) that activates Rap1 to promote cell adhesion. Resting C3G is autoinhibited and the GEF activity is released by stimuli that signal through tyrosine kinases. C3G is activated by tyrosine phosphorylation and interaction with Crk adaptor proteins, whose expression is elevated in multiple human cancers. However, the molecular details of C3G activation and the interplay between phosphorylation and Crk interaction are poorly understood. Methods: We combined biochemical, biophysical, and cell biology approaches to elucidate the mechanisms of C3G activation. Binding of Crk adaptor proteins to four proline-rich motifs (P1 to P4) in C3G was characterized in vitro using isothermal titration calorimetry and sedimentation velocity, and in Jurkat and HEK293T cells by affinity pull-down assays. The nucleotide exchange activity of C3G over Rap1 was measured using nucleotide-dissociation kinetic assays. Jurkat cells were also used to analyze C3G translocation to the plasma membrane and the C3G-dependent activation of Rap1 upon ligation of T cell receptors. Results: CrkL interacts through its SH3N domain with sites P1 and P2 of inactive C3G in vitro and in Jurkat and HEK293T cells, and these sites are necessary to recruit C3G to the plasma membrane. However, direct stimulation of the GEF activity requires binding of Crk proteins to the P3 and P4 sites. P3 is occluded in resting C3G and is essential for activation, while P4 contributes secondarily towards complete stimulation. Tyrosine phosphorylation of C3G alone causes marginal activation. Instead, phosphorylation primes C3G lowering the concentration of Crk proteins required for activation and increasing the maximum activity. Unexpectedly, optimal activation also requires the interaction of CrkL-SH2 domain with phosphorylated C3G. Conclusion: Our study revealed that phosphorylation of C3G by Src and Crk-binding form a two-factor mechanism that ensures tight control of C3G activation. Additionally, the simultaneous SH2 and SH3N interaction of CrkL with C3G, required for the activation, reveals a novel adaptor-independent function of Crk proteins relevant to understanding their role in physiological signaling and their deregulation in diseases. Video abstract.
MeSH term(s)	Humans ; Guanine Nucleotide Exchange Factors/metabolism ; Guanine Nucleotide-Releasing Factor 2/metabolism ; HEK293 Cells ; Nuclear Proteins/metabolism ; Nucleotides/metabolism ; Proto-Oncogene Proteins c-crk/metabolism ; src Homology Domains ; Tyrosine/metabolism
Chemical Substances	CRK protein, human ; Guanine Nucleotide Exchange Factors ; Guanine Nucleotide-Releasing Factor 2 ; Nuclear Proteins ; Nucleotides ; Proto-Oncogene Proteins c-crk ; Tyrosine (42HK56048U) ; TERF2IP protein, human
Language	English
Publishing date	2023-02-03
Publishing country	England
Document type	Video-Audio Media ; Journal Article ; Research Support, N.I.H., Intramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2126315-2
ISSN	1478-811X ; 1478-811X
ISSN (online)	1478-811X
ISSN	1478-811X
DOI	10.1186/s12964-023-01042-2
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Article ; Online: Correction: Analysis of gene variants in the GASH/Sal model of epilepsy.

Díaz-Casado, Elena / Gómez-Nieto, Ricardo / de Pereda, José M / Muñoz, Luis J / Jara-Acevedo, María / López, Dolores E

PloS one

2020 Volume 15, Issue 4, Page(s) e0231603

Abstract: This corrects the article DOI: 10.1371/journal.pone.0229953.]. ...

Abstract	[This corrects the article DOI: 10.1371/journal.pone.0229953.].
Language	English
Publishing date	2020-04-03
Publishing country	United States
Document type	Published Erratum
ISSN	1932-6203
ISSN (online)	1932-6203
DOI	10.1371/journal.pone.0231603
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Article ; Online: Crk proteins activate the Rap1 guanine nucleotide exchange factor C3G by segregated adaptor-dependent and -independent mechanisms

Antonio Rodríguez-Blázquez / Arturo Carabias / Alba Morán-Vaquero / Sergio de Cima / Juan R. Luque-Ortega / Carlos Alfonso / Peter Schuck / José Antonio Manso / Sandra Macedo-Ribeiro / Carmen Guerrero / José M. de Pereda

Cell Communication and Signaling, Vol 21, Iss 1, Pp 1-

2023 Volume 22

Abstract: Abstract Background C3G is a guanine nucleotide exchange factor (GEF) that activates Rap1 to promote cell adhesion. Resting C3G is autoinhibited and the GEF activity is released by stimuli that signal through tyrosine kinases. C3G is activated by ... ...

Abstract	Abstract Background C3G is a guanine nucleotide exchange factor (GEF) that activates Rap1 to promote cell adhesion. Resting C3G is autoinhibited and the GEF activity is released by stimuli that signal through tyrosine kinases. C3G is activated by tyrosine phosphorylation and interaction with Crk adaptor proteins, whose expression is elevated in multiple human cancers. However, the molecular details of C3G activation and the interplay between phosphorylation and Crk interaction are poorly understood. Methods We combined biochemical, biophysical, and cell biology approaches to elucidate the mechanisms of C3G activation. Binding of Crk adaptor proteins to four proline-rich motifs (P1 to P4) in C3G was characterized in vitro using isothermal titration calorimetry and sedimentation velocity, and in Jurkat and HEK293T cells by affinity pull-down assays. The nucleotide exchange activity of C3G over Rap1 was measured using nucleotide-dissociation kinetic assays. Jurkat cells were also used to analyze C3G translocation to the plasma membrane and the C3G-dependent activation of Rap1 upon ligation of T cell receptors. Results CrkL interacts through its SH3N domain with sites P1 and P2 of inactive C3G in vitro and in Jurkat and HEK293T cells, and these sites are necessary to recruit C3G to the plasma membrane. However, direct stimulation of the GEF activity requires binding of Crk proteins to the P3 and P4 sites. P3 is occluded in resting C3G and is essential for activation, while P4 contributes secondarily towards complete stimulation. Tyrosine phosphorylation of C3G alone causes marginal activation. Instead, phosphorylation primes C3G lowering the concentration of Crk proteins required for activation and increasing the maximum activity. Unexpectedly, optimal activation also requires the interaction of CrkL-SH2 domain with phosphorylated C3G. Conclusion Our study revealed that phosphorylation of C3G by Src and Crk-binding form a two-factor mechanism that ensures tight control of C3G activation. Additionally, the ...
Keywords	Ras-associated protein 1 ; RapGEF1 ; Signal transduction ; Tyrosine phosphorylation ; Src-homology 2 domain ; Src-homology 3 domain ; Medicine ; R ; Cytology ; QH573-671
Subject code	570
Language	English
Publishing date	2023-02-01T00:00:00Z
Publisher	BMC
Document type	Article ; Online
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Article ; Online: PSTPIP1-LYP phosphatase interaction: structural basis and implications for autoinflammatory disorders.

Manso, José A / Marcos, Tamara / Ruiz-Martín, Virginia / Casas, Javier / Alcón, Pablo / Sánchez Crespo, Mariano / Bayón, Yolanda / de Pereda, José M / Alonso, Andrés

Cellular and molecular life sciences : CMLS

2022 Volume 79, Issue 2, Page(s) 131

Abstract: Mutations in the adaptor protein PSTPIP1 cause a spectrum of autoinflammatory diseases, including PAPA and PAMI; however, the mechanism underlying these diseases remains unknown. Most of these mutations lie in PSTPIP1 F-BAR domain, which binds to LYP, a ... ...

Abstract	Mutations in the adaptor protein PSTPIP1 cause a spectrum of autoinflammatory diseases, including PAPA and PAMI; however, the mechanism underlying these diseases remains unknown. Most of these mutations lie in PSTPIP1 F-BAR domain, which binds to LYP, a protein tyrosine phosphatase associated with arthritis and lupus. To shed light on the mechanism by which these mutations generate autoinflammatory disorders, we solved the structure of the F-BAR domain of PSTPIP1 alone and bound to the C-terminal homology segment of LYP, revealing a novel mechanism of recognition of Pro-rich motifs by proteins in which a single LYP molecule binds to the PSTPIP1 F-BAR dimer. The residues R228, D246, E250, and E257 of PSTPIP1 that are mutated in immunological diseases directly interact with LYP. These findings link the disruption of the PSTPIP1/LYP interaction to these diseases, and support a critical role for LYP phosphatase in their pathogenesis.
MeSH term(s)	Adaptor Proteins, Signal Transducing/chemistry ; Adaptor Proteins, Signal Transducing/genetics ; Adaptor Proteins, Signal Transducing/physiology ; Crystallization ; Cytoskeletal Proteins/chemistry ; Cytoskeletal Proteins/genetics ; Cytoskeletal Proteins/physiology ; Diabetes Mellitus, Type 1/etiology ; HEK293 Cells ; Humans ; Immune System Diseases/etiology ; Mutation ; Protein Domains ; Protein Multimerization ; Protein Tyrosine Phosphatase, Non-Receptor Type 22/chemistry ; Protein Tyrosine Phosphatase, Non-Receptor Type 22/genetics ; Protein Tyrosine Phosphatase, Non-Receptor Type 22/physiology
Chemical Substances	Adaptor Proteins, Signal Transducing ; Cytoskeletal Proteins ; PSTPIP1 protein, human ; Protein Tyrosine Phosphatase, Non-Receptor Type 22 (EC 3.1.3.48)
Language	English
Publishing date	2022-02-12
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	1358415-7
ISSN	1420-9071 ; 1420-682X
ISSN (online)	1420-9071
ISSN	1420-682X
DOI	10.1007/s00018-022-04173-w
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Article ; Online: EGFR-dependent tyrosine phosphorylation of integrin β4 is not required for downstream signaling events in cancer cell lines.

Te Molder, Lisa / Kreft, Maaike / Heemskerk, Niels / Schuring, Joyce / de Pereda, Jose M / Wilhelmsen, Kevin / Sonnenberg, Arnoud

Scientific reports

2021 Volume 11, Issue 1, Page(s) 8675

Abstract: In epithelial cancers, the epidermal growth factor receptor (EGFR) and integrin α6β4 are frequently overexpressed and found to synergistically activate intracellular signaling pathways that promote cell proliferation and migration. In cancer cells, the ... ...

Abstract	In epithelial cancers, the epidermal growth factor receptor (EGFR) and integrin α6β4 are frequently overexpressed and found to synergistically activate intracellular signaling pathways that promote cell proliferation and migration. In cancer cells, the β4 subunit is phosphorylated at tyrosine residues not normally recognized as kinase substrates; however, the function of these phosphotyrosine residues in cancer cells is a subject of much debate. In EGFR-overexpressing carcinoma cells, we found that the Src family kinase (SFK) inhibitor PP2 reduces β4 tyrosine phosphorylation following the activation of EGFR. However, siRNA mediated knockdown of the SFKs Src, Fyn, Yes and Lyn, individually or in combination, did not affect the EGF-induced phosphorylation of β4. Using phospho-peptide affinity chromatography and mass spectrometry, we found that PLCγ1 binds β4 at the phosphorylated residues Y1422/Y1440, but were unable to verify this interaction in A431 carcinoma cells that overexpress the EGFR. Furthermore, using A431 cells devoid of β4 or reconstituted with phenylalanine specific mutants of β4, the activation of several downstream signaling pathways, including PLCγ/PKC, MAPK and PI3K/Akt, were not substantially affected. We conclude that tyrosine-phosphorylated β4 does not enhance EGFR-mediated signaling in EGFR-overexpressing cells, despite the fact that this integrin subunit is highly tyrosine phosphorylated in these cells.
MeSH term(s)	Animals ; Cell Line, Tumor ; Gene Expression Regulation, Neoplastic/genetics ; Humans ; Integrin beta4/metabolism ; Integrin beta4/physiology ; Mass Spectrometry ; Phosphorylation ; Phosphotyrosine/metabolism ; Reverse Transcriptase Polymerase Chain Reaction ; Signal Transduction ; Skin Neoplasms/genetics ; Skin Neoplasms/metabolism ; Tyrosine/metabolism
Chemical Substances	Integrin beta4 ; Phosphotyrosine (21820-51-9) ; Tyrosine (42HK56048U)
Language	English
Publishing date	2021-04-21
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-021-88134-6
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Article: PSTPIP1-LYP phosphatase interaction: structural basis and implications for autoinflammatory disorders

Manso, José A. / Marcos, Tamara / Ruiz-Martín, Virginia / Casas, Javier / Alcón, Pablo / Sánchez Crespo, Mariano / Bayón, Yolanda / de Pereda, José M. / Alonso, Andrés

Cellular and molecular life sciences. 2022 Feb., v. 79, no. 2

2022

Abstract	Mutations in the adaptor protein PSTPIP1 cause a spectrum of autoinflammatory diseases, including PAPA and PAMI; however, the mechanism underlying these diseases remains unknown. Most of these mutations lie in PSTPIP1 F-BAR domain, which binds to LYP, a protein tyrosine phosphatase associated with arthritis and lupus. To shed light on the mechanism by which these mutations generate autoinflammatory disorders, we solved the structure of the F-BAR domain of PSTPIP1 alone and bound to the C-terminal homology segment of LYP, revealing a novel mechanism of recognition of Pro-rich motifs by proteins in which a single LYP molecule binds to the PSTPIP1 F-BAR dimer. The residues R228, D246, E250, and E257 of PSTPIP1 that are mutated in immunological diseases directly interact with LYP. These findings link the disruption of the PSTPIP1/LYP interaction to these diseases, and support a critical role for LYP phosphatase in their pathogenesis.
Keywords	arthritis ; pathogenesis ; protein-tyrosine-phosphatase
Language	English
Dates of publication	2022-02
Size	p. 131.
Publishing place	Springer International Publishing
Document type	Article
ZDB-ID	1358415-7
ISSN	1420-9071 ; 1420-682X
ISSN (online)	1420-9071
ISSN	1420-682X
DOI	10.1007/s00018-022-04173-w
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Article ; Online: Correction

Elena Díaz-Casado / Ricardo Gómez-Nieto / José M de Pereda / Luis J Muñoz / María Jara-Acevedo / Dolores E López

PLoS ONE, Vol 15, Iss 4, p e

Analysis of gene variants in the GASH/Sal model of epilepsy.

2020 Volume 0231603

Abstract: This corrects the article DOI:10.1371/journal.pone.0229953.]. ...

Abstract	[This corrects the article DOI:10.1371/journal.pone.0229953.].
Keywords	Medicine ; R ; Science ; Q
Language	English
Publishing date	2020-01-01T00:00:00Z
Publisher	Public Library of Science (PLoS)
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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