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Article ; Online: Antibiotics inhibit tumor and disease activity in cutaneous T-cell lymphoma.

Lindahl, Lise M / Willerslev-Olsen, Andreas / Gjerdrum, Lise M R / Nielsen, Pia R / Blümel, Edda / Rittig, Anne H / Celis, Pamela / Herpers, Bjorn / Becker, Jürgen C / Stausbøl-Grøn, Birgitte / Wasik, Mariusz A / Gluud, Maria / Fredholm, Simon / Buus, Terkild B / Johansen, Claus / Nastasi, Claudia / Peiffer, Lukas / Kubat, Linda / Bzorek, Michael /

Eriksen, Jens O / Krejsgaard, Thorbjørn / Bonefeld, Charlotte M / Geisler, Carsten / Mustelin, Tomas / Langhoff, Erik / Givskov, Michael / Woetmann, Anders / Kilian, Mogens / Litman, Thomas / Iversen, Lars / Odum, Niels

Blood

2019 Volume 134, Issue 13, Page(s) 1072–1083

Abstract: It has been proposed that CD4 T-cell responses to ...

Abstract	It has been proposed that CD4 T-cell responses to
MeSH term(s)	Aged ; Anti-Bacterial Agents/therapeutic use ; Cell Proliferation/drug effects ; Female ; Humans ; Lymphoma, T-Cell, Cutaneous/drug therapy ; Lymphoma, T-Cell, Cutaneous/metabolism ; Lymphoma, T-Cell, Cutaneous/pathology ; Male ; Middle Aged ; Prospective Studies ; STAT3 Transcription Factor/metabolism ; Signal Transduction/drug effects ; Skin Neoplasms/drug therapy ; Skin Neoplasms/metabolism ; Skin Neoplasms/pathology ; T-Lymphocytes/drug effects ; T-Lymphocytes/metabolism ; T-Lymphocytes/pathology
Chemical Substances	Anti-Bacterial Agents ; STAT3 Transcription Factor ; STAT3 protein, human
Language	English
Publishing date	2019-07-22
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	80069-7
ISSN	1528-0020 ; 0006-4971
ISSN (online)	1528-0020
ISSN	0006-4971
DOI	10.1182/blood.2018888107
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Book ; Thesis: Transduction of mitogenic signals in T-lymphocytes inositide turnover and rapid activation of ornithine decarboxylase

Mustelin, Tomas

1987

Author's details	Tomas Mustelin
Keywords	Ornithine Decarboxylase ; Stimulation, Chemical ; Mitogens ; T-Lymphocytes ; Transduction, Genetic
Language	English
Size	78 S. : Ill., graph. Darst.
Publishing country	Finland
Document type	Book ; Thesis
Thesis / German Habilitation thesis	Helsinki, Univ., Diss., 1987
HBZ-ID	HT003191943
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Article ; Online: Immunology. Restless T cells sniff and go.

Mustelin, Tomas

Science (New York, N.Y.)

2006 Volume 313, Issue 5795, Page(s) 1902–1903

MeSH term(s)	Animals ; Antigen Presentation ; Antigens, CD ; Antigens, Differentiation/genetics ; Antigens, Differentiation/physiology ; Autoimmunity ; B7-1 Antigen/metabolism ; B7-2 Antigen/metabolism ; CD28 Antigens/metabolism ; CTLA-4 Antigen ; Cell Adhesion ; Cell Movement ; Dendritic Cells/immunology ; Humans ; Integrins/physiology ; Ligands ; Lymph Nodes/immunology ; Lymphocyte Activation ; Mice ; Receptors, Antigen, T-Cell/immunology ; Receptors, Antigen, T-Cell/metabolism ; Signal Transduction ; T-Lymphocytes/immunology ; T-Lymphocytes/physiology
Chemical Substances	Antigens, CD ; Antigens, Differentiation ; B7-1 Antigen ; B7-2 Antigen ; CD28 Antigens ; CTLA-4 Antigen ; CTLA4 protein, human ; Ctla4 protein, mouse ; Integrins ; Ligands ; Receptors, Antigen, T-Cell
Language	English
Publishing date	2006-09-29
Publishing country	United States
Document type	Journal Article ; Comment
ZDB-ID	128410-1
ISSN	1095-9203 ; 0036-8075
ISSN (online)	1095-9203
ISSN	0036-8075
DOI	10.1126/science.1133578
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Article ; Online: LYP inhibits T-cell activation when dissociated from CSK.

Vang, Torkel / Liu, Wallace H / Delacroix, Laurence / Wu, Shuangding / Vasile, Stefan / Dahl, Russell / Yang, Li / Musumeci, Lucia / Francis, Dana / Landskron, Johannes / Tasken, Kjetil / Tremblay, Michel L / Lie, Benedicte A / Page, Rebecca / Mustelin, Tomas / Rahmouni, Souad / Rickert, Robert C / Tautz, Lutz

Nature chemical biology

2012 Volume 8, Issue 5, Page(s) 437–446

Abstract: ... of signaling mediated through the T-cell antigen receptor (TCR) and are thought to act in a cooperative manner ... when forming a complex. Here we studied the spatiotemporal dynamics of the LYP-CSK complex in T ... inhibits T-cell activation when removed from CSK. Our findings may explain the reduced TCR-mediated ...

Abstract	Lymphoid tyrosine phosphatase (LYP) and C-terminal Src kinase (CSK) are negative regulators of signaling mediated through the T-cell antigen receptor (TCR) and are thought to act in a cooperative manner when forming a complex. Here we studied the spatiotemporal dynamics of the LYP-CSK complex in T cells. We demonstrate that dissociation of this complex is necessary for recruitment of LYP to the plasma membrane, where it downmodulates TCR signaling. Development of a potent and selective chemical probe of LYP confirmed that LYP inhibits T-cell activation when removed from CSK. Our findings may explain the reduced TCR-mediated signaling associated with a single-nucleotide polymorphism that confers increased risk for certain autoimmune diseases, including type 1 diabetes and rheumatoid arthritis, and results in expression of a mutant LYP that is unable to bind CSK. Our compound also represents a starting point for the development of a LYP-based treatment of autoimmunity.
MeSH term(s)	CSK Tyrosine-Protein Kinase ; Cell Membrane/metabolism ; Down-Regulation ; Humans ; Lymphocyte Activation ; Protein Binding ; Protein Tyrosine Phosphatase, Non-Receptor Type 22/metabolism ; Protein-Tyrosine Kinases/metabolism ; Receptors, Antigen, T-Cell/metabolism ; Signal Transduction ; T-Lymphocytes/metabolism ; src-Family Kinases
Chemical Substances	Receptors, Antigen, T-Cell ; Protein-Tyrosine Kinases (EC 2.7.10.1) ; CSK Tyrosine-Protein Kinase (EC 2.7.10.2) ; src-Family Kinases (EC 2.7.10.2) ; CSK protein, human (EC 2.7.10.23) ; PTPN22 protein, human (EC 3.1.3.48) ; Protein Tyrosine Phosphatase, Non-Receptor Type 22 (EC 3.1.3.48)
Language	English
Publishing date	2012-03-18
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2202962-X
ISSN	1552-4469 ; 1552-4450
ISSN (online)	1552-4469
ISSN	1552-4450
DOI	10.1038/nchembio.916
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Article ; Online: The autoimmune-predisposing variant of lymphoid tyrosine phosphatase favors T helper 1 responses.

Vang, Torkel / Landskron, Johannes / Viken, Marte K / Oberprieler, Nikolaus / Torgersen, Knut M / Mustelin, Tomas / Tasken, Kjetil / Tautz, Lutz / Rickert, Robert C / Lie, Benedicte A

Human immunology

2013 Volume 74, Issue 5, Page(s) 574–585

Abstract: ... we compared both T cell signaling and T cell function in healthy human donors homozygous for either LYP*R620 ... or LYP*W620. Generally, the presence of LYP*W620 caused reduced proximal T cell antigen receptor ... expressing either LYP*R620 or LYP*W620 also affected the differentiation of conventional CD4(+) T ...

Abstract	The C1858T single nucleotide polymorphism in PTPN22, which is the gene encoding lymphoid tyrosine phosphatase (LYP), confers increased risk for various autoimmune disorders in Caucasians. Although the disease-associated LYP allele (LYPW620) is a gain-of-function variant that has higher catalytic activity than the major allele (LYPR620), it is still unclear how LYPW620 predisposes for autoimmunity. Here, we compared both T cell signaling and T cell function in healthy human donors homozygous for either LYPR620 or LYPW620. Generally, the presence of LYPW620 caused reduced proximal T cell antigen receptor-mediated signaling (e.g. ζ chain phosphorylation) but augmented CD28-associated signaling (e.g. AKT activation). Altered ligand binding properties of the two LYP variants could explain these findings since LYPR620 interacted more strongly with the p85 subunit of PI3K. Variation in signaling between cells expressing either LYPR620 or LYPW620 also affected the differentiation of conventional CD4(+) T cells. For example, LYPW620 homozygous donors displayed exaggerated Th1 responses (e.g. IFNγ production) and reduced Th17 responses (e.g. IL-17 production). Importantly, while regulatory T cells normally suppressed Th1-mediated IFNγ production in LYPR620 homozygous individuals, such suppression was lost in LYPW620 homozygous individuals. Altogether, these findings provide a molecular and cellular explanation for the autoimmune phenotype associated with LYP*W620.
MeSH term(s)	Adult ; Alleles ; Autoimmune Diseases/genetics ; Female ; Flow Cytometry ; Genetic Predisposition to Disease/genetics ; Genotype ; HEK293 Cells ; Humans ; Interferon-gamma/immunology ; Interferon-gamma/metabolism ; Interleukin-17/immunology ; Interleukin-17/metabolism ; Jurkat Cells ; Male ; Middle Aged ; Phosphatidylinositol 3-Kinases/immunology ; Phosphatidylinositol 3-Kinases/metabolism ; Phosphorylation/immunology ; Polymorphism, Single Nucleotide ; Protein Tyrosine Phosphatase, Non-Receptor Type 22/genetics ; Proto-Oncogene Proteins c-akt/immunology ; Proto-Oncogene Proteins c-akt/metabolism ; Receptors, Antigen, T-Cell/immunology ; Receptors, Antigen, T-Cell/metabolism ; Signal Transduction/immunology ; Th1 Cells/immunology ; Th1 Cells/metabolism ; Th17 Cells/immunology ; Th17 Cells/metabolism
Chemical Substances	Interleukin-17 ; Receptors, Antigen, T-Cell ; antigen T cell receptor, zeta chain ; Interferon-gamma (82115-62-6) ; Phosphatidylinositol 3-Kinases (EC 2.7.1.-) ; Proto-Oncogene Proteins c-akt (EC 2.7.11.1) ; PTPN22 protein, human (EC 3.1.3.48) ; Protein Tyrosine Phosphatase, Non-Receptor Type 22 (EC 3.1.3.48)
Language	English
Publishing date	2013-01-17
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	801524-7
ISSN	1879-1166 ; 0198-8859
ISSN (online)	1879-1166
ISSN	0198-8859
DOI	10.1016/j.humimm.2012.12.017
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Article: Role of protein tyrosine phosphatases in T cell activation.

Mustelin, Tomas / Rahmouni, Souad / Bottini, Nunzio / Alonso, Andres

Immunological reviews

2003 Volume 191, Page(s) 139–147

Abstract: ... of signal transduction. In T cells, much of the focus has been on protein tyrosine kinase (PTK)-mediated signaling ... from the T cell receptor (TCR) and cytokine receptors, while the study of protein tyrosine phosphatases ... roles in many different aspects of T cell physiology. We predict that the phosphatases will become ...

Abstract	The last decade has seen an exponentially increasing interest in the molecular mechanisms of signal transduction. In T cells, much of the focus has been on protein tyrosine kinase (PTK)-mediated signaling from the T cell receptor (TCR) and cytokine receptors, while the study of protein tyrosine phosphatases (PTPases) has lagged behind. However, recent discoveries have revealed that several PTPases play important roles in many different aspects of T cell physiology. We predict that the phosphatases will become a 'hot topic' in the field within the next few years. This review summarizes the current understanding of the regulation and biology of PTPases in T lymphocyte activation.
MeSH term(s)	Animals ; Autoimmune Diseases/metabolism ; Humans ; Leukocyte Common Antigens/physiology ; Protein Tyrosine Phosphatases/physiology ; Signal Transduction/physiology ; T-Lymphocytes/enzymology
Chemical Substances	Leukocyte Common Antigens (EC 3.1.3.48) ; Protein Tyrosine Phosphatases (EC 3.1.3.48)
Language	English
Publishing date	2003-01-28
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S. ; Review
ZDB-ID	391796-4
ISSN	1600-065X ; 0105-2896
ISSN (online)	1600-065X
ISSN	0105-2896
DOI	10.1034/j.1600-065x.2003.00014.x
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Article ; Online: Prediction of alternative pre-mRNA splicing outcomes.

Najjar, Rayan / Mustelin, Tomas

Scientific reports

2023 Volume 13, Issue 1, Page(s) 20000

Abstract: To understand the biological impact of alternative pre-mRNA splicing, it is vital to know which exons are involved, what protein domains they encode, and how the translated isoforms differ. Therefore, we developed a computational pipeline (RiboSplitter) ... ...

Abstract	To understand the biological impact of alternative pre-mRNA splicing, it is vital to know which exons are involved, what protein domains they encode, and how the translated isoforms differ. Therefore, we developed a computational pipeline (RiboSplitter) focused on functional effect prediction. It builds on event-based alternative splicing detection with additional filtering steps leading to more efficient statistical testing, and with detection of isoform-specific protein changes. A key methodological advance is reading frame prediction by translating exonic DNA in all possible frames, then finding a single open reading frame, or a single frame with matches to known proteins of the gene. This allowed unambiguous translation in 93.9% of alternative splicing events when tested on RNA-sequencing data of B cells from Sjögren's syndrome patients. RiboSplitter does not depend on reference annotations and translates events even when one or both isoform(s) are novel (unannotated). RiboSplitter's visualizations illustrate each event with translation outcomes, show event location within the gene, and align exons to protein domains.
MeSH term(s)	Humans ; RNA Precursors/genetics ; RNA Precursors/metabolism ; RNA, Messenger/genetics ; RNA Splicing/genetics ; Alternative Splicing ; Protein Isoforms/metabolism
Chemical Substances	RNA Precursors ; RNA, Messenger ; Protein Isoforms
Language	English
Publishing date	2023-11-15
Publishing country	England
Document type	Journal Article
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-023-47348-6
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Article: Protein tyrosine phosphatases in T cell physiology.

Mustelin, Tomas / Alonso, Andres / Bottini, Nunzio / Huynh, Huong / Rahmouni, Souad / Nika, Konstantina / Louis-dit-Sully, Christine / Tautz, Lutz / Togo, Summanuna H / Bruckner, Shane / Mena-Duran, Armando V / al-Khouri, Anna Maria

Molecular immunology

2004 Volume 41, Issue 6-7, Page(s) 687–700

Abstract: ... the last decade. In T cells, much of the work has centered on protein tyrosine kinase-mediated signaling ... Nevertheless, it has now become clear that many protein tyrosine phosphatases play equally important roles in T ... of protein tyrosine phosphatases in T lymphocyte physiology. ...

Abstract	The molecular mechanisms of signal transduction have been the focus of intense research during the last decade. In T cells, much of the work has centered on protein tyrosine kinase-mediated signaling from the TCR and cytokine receptors, while the study of protein tyrosine phosphatases has lagged behind. Nevertheless, it has now become clear that many protein tyrosine phosphatases play equally important roles in T cell physiology and that no kinase-regulated system would work without the counterbalancing participation of phosphatases. In fact, we have learned that many processes are regulated primarily on the phosphatase side. This minireview summarizes the current state-of-the art in our understanding of the regulation and biology of protein tyrosine phosphatases in T lymphocyte physiology.
MeSH term(s)	Dual Specificity Phosphatase 3 ; Endoplasmic Reticulum/physiology ; Humans ; Leukocyte Common Antigens/immunology ; Leukocyte Common Antigens/physiology ; Mitogen-Activated Protein Kinases/immunology ; Mitogen-Activated Protein Kinases/physiology ; Phosphorylation ; Protein Tyrosine Phosphatases/immunology ; Protein Tyrosine Phosphatases/physiology ; T-Lymphocytes/enzymology ; T-Lymphocytes/immunology ; src-Family Kinases/immunology ; src-Family Kinases/physiology
Chemical Substances	src-Family Kinases (EC 2.7.10.2) ; Mitogen-Activated Protein Kinases (EC 2.7.11.24) ; DUSP3 protein, human (EC 3.1.3.48) ; Dual Specificity Phosphatase 3 (EC 3.1.3.48) ; Leukocyte Common Antigens (EC 3.1.3.48) ; Protein Tyrosine Phosphatases (EC 3.1.3.48)
Language	English
Publishing date	2004-07
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S. ; Review
ZDB-ID	424427-8
ISSN	1872-9142 ; 0161-5890
ISSN (online)	1872-9142
ISSN	0161-5890
DOI	10.1016/j.molimm.2004.04.015
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Article: Protein tyrosine phosphorylation in T cell signaling.

Mustelin, Tomas / Abraham, Robert T / Rudd, Christopher E / Alonso, Andres / Merlo, Joseph J

Frontiers in bioscience : a journal and virtual library

2002 Volume 7, Page(s) d918–69

Abstract: This review discusses in considerable detail the tyrosine phosphorylation events that couple the T ... of phosphate from tyrosine residues. Next, we discuss the molecular clock work by which these enzymes initiated T cell ... in coupling the kinases and phosphatases to gene transcription and other aspects of the T lymphocyte response ...

Abstract	This review discusses in considerable detail the tyrosine phosphorylation events that couple the T cell antigen receptor to downstream signaling pathways. First, the protein kinases that catalyze these tyrosine phosphorylation are introduced, then the phosphatases that mediate removal of phosphate from tyrosine residues. Next, we discuss the molecular clock work by which these enzymes initiated T cell activation. Finally, we briefly review the key substrates for tyrosine phosphorylation and their role in coupling the kinases and phosphatases to gene transcription and other aspects of the T lymphocyte response to antigen.
MeSH term(s)	Animals ; Enzyme Precursors/metabolism ; Intracellular Signaling Peptides and Proteins ; Lymphocyte Activation ; Phosphoproteins/metabolism ; Phosphorylation ; Phosphotyrosine/metabolism ; Protein Tyrosine Phosphatases/metabolism ; Protein-Tyrosine Kinases/chemistry ; Protein-Tyrosine Kinases/metabolism ; Receptors, Antigen, T-Cell/metabolism ; Signal Transduction ; Syk Kinase ; T-Lymphocytes/enzymology ; T-Lymphocytes/immunology ; src-Family Kinases/chemistry ; src-Family Kinases/metabolism
Chemical Substances	Enzyme Precursors ; Intracellular Signaling Peptides and Proteins ; Phosphoproteins ; Receptors, Antigen, T-Cell ; Phosphotyrosine (21820-51-9) ; Tec protein-tyrosine kinase (EC 2.7.1.-) ; Protein-Tyrosine Kinases (EC 2.7.10.1) ; Syk Kinase (EC 2.7.10.2) ; src-Family Kinases (EC 2.7.10.2) ; Protein Tyrosine Phosphatases (EC 3.1.3.48)
Language	English
Publishing date	2002-04-01
Publishing country	United States
Document type	Journal Article ; Research Support, U.S. Gov't, P.H.S. ; Review
ZDB-ID	2141320-4
ISSN	1093-9946
ISSN	1093-9946
DOI	10.2741/A821
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Article: Positive and negative regulation of T-cell activation through kinases and phosphatases.

Mustelin, Tomas / Taskén, Kjetil

The Biochemical journal

2003 Volume 371, Issue Pt 1, Page(s) 15–27

Abstract: The sequence of events in T-cell antigen receptor (TCR) signalling leading to T-cell activation ... phosphorylation and thereby on activation and proliferation of T-cells. This review focuses on the involvement ... of PTKs and PTPases in positive and negative regulation of T-cell activation, the emerging theme ...

Abstract	The sequence of events in T-cell antigen receptor (TCR) signalling leading to T-cell activation involves regulation of a number of protein tyrosine kinases (PTKs) and the phosphorylation status of many of their substrates. Proximal signalling pathways involve PTKs of the Src, Syk, Csk and Tec families, adapter proteins and effector enzymes in a highly organized tyrosine-phosphorylation cascade. In intact cells, tyrosine phosphorylation is rapidly reversible and generally of a very low stoichiometry even under induced conditions due to the fact that the enzymes removing phosphate from tyrosine-phosphorylated substrates, the protein tyrosine phosphatases (PTPases), have a capacity that is several orders of magnitude higher than that of the PTKs. It follows that a relatively minor change in the PTK/PTPase balance can have a major impact on net tyrosine phosphorylation and thereby on activation and proliferation of T-cells. This review focuses on the involvement of PTKs and PTPases in positive and negative regulation of T-cell activation, the emerging theme of reciprocal regulation of each type of enzyme by the other, as well as regulation of phosphotyrosine turnover by Ser/Thr phosphorylation and regulation of localization of signal components.
MeSH term(s)	Animals ; Humans ; Isoenzymes/metabolism ; Leukocyte Common Antigens/metabolism ; Lymphocyte Activation/physiology ; Lymphocyte Specific Protein Tyrosine Kinase p56(lck)/metabolism ; Phosphoric Monoester Hydrolases/metabolism ; Phosphotransferases/metabolism ; Protein Tyrosine Phosphatase, Non-Receptor Type 12 ; Protein Tyrosine Phosphatases/metabolism ; Protein-Tyrosine Kinases/metabolism ; Proto-Oncogene Proteins/metabolism ; Proto-Oncogene Proteins c-fyn ; Receptors, Antigen, T-Cell/metabolism ; Signal Transduction/physiology ; ZAP-70 Protein-Tyrosine Kinase ; src-Family Kinases/metabolism
Chemical Substances	Isoenzymes ; Proto-Oncogene Proteins ; Receptors, Antigen, T-Cell ; Phosphotransferases (EC 2.7.-) ; Protein-Tyrosine Kinases (EC 2.7.10.1) ; CSK tyrosine-protein kinase (EC 2.7.10.2) ; FYN protein, human (EC 2.7.10.2) ; Lymphocyte Specific Protein Tyrosine Kinase p56(lck) (EC 2.7.10.2) ; Proto-Oncogene Proteins c-fyn (EC 2.7.10.2) ; ZAP-70 Protein-Tyrosine Kinase (EC 2.7.10.2) ; ZAP70 protein, human (EC 2.7.10.2) ; src-Family Kinases (EC 2.7.10.2) ; Phosphoric Monoester Hydrolases (EC 3.1.3.2) ; ACP1 protein, human (EC 3.1.3.48) ; Leukocyte Common Antigens (EC 3.1.3.48) ; PTPN12 protein, human (EC 3.1.3.48) ; Protein Tyrosine Phosphatase, Non-Receptor Type 12 (EC 3.1.3.48) ; Protein Tyrosine Phosphatases (EC 3.1.3.48)
Language	English
Publishing date	2003-04-01
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	2969-5
ISSN	1470-8728 ; 0264-6021 ; 0006-2936 ; 0306-3275
ISSN (online)	1470-8728
ISSN	0264-6021 ; 0006-2936 ; 0306-3275
DOI	10.1042/BJ20021637
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