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Balbino Alarcón

Centro de Biología Molecular Severo Ochoa

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Co-Authors

Aldo Borroto

Centro de Biología Molecular Severo Ochoa

Wolfgang W. Schamel

University Medical Center Freiburg

Xosé R. Bustelo

Centro de Investigación del Cáncer

Manuel Fresno

Universidad Autónoma de Madrid

Cox Terhorst

Beth Israel Deaconess Medical Center

Clara L. Oeste

Universidad Autónoma de Madrid

Pilar Delgado

Universidad Autónoma de Madrid

Luis Carrasco

Universidad Autónoma de Madrid

Hisse M. van Santen

Consejo Superior de Investigaciones Científicas

Francisco Sánchez‐Madrid

Universidad Autónoma de Madrid

Cooperative Institutions

Consejo Superior de Investigaciones Científicas

Universidad Autónoma de Madrid

Centro de Biología Molecular Severo Ochoa

Instituto de Salud Carlos III

Universidad Complutense de Madrid

Centro de Investigación Biomédica en Red

Centro de Investigación del Cáncer

Universidad de Salamanca

Research Institute Hospital 12 de Octubre

Centro Nacional de Biotecnología

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Citation

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1H‐NMR analysis of CD3‐ε reveals the presence of turn‐helix structures around the ITAM motif in an otherwise random coil cytoplasmic tail

Biopolymers (1997)

Aldo Borroto Mercedes Jiménez Balbino Alarcón Manuel Rico

The conformation adopted in solution by the cytoplasmic tail of CD3-ϵ has been analyzed by 1H-nmr. The cytoplasmic tail is mostly random coil except for the amino acids conforming the immunoreceptor tyrosine-based activation motif (ITAM), YxxL/IxxxxxxxY xxL. Although the N-terminal Y xxL sequence of the motif is poorly folded, adopting 6-residue turn-like conformations with the Tyr side chain in two different orientations, the C-terminal Y xxL sequence is placed in a more complex structure involving a set of nonclassical α-helix turns and β-turns that comprises 11 amino acids. This structure is not modified by phosphorylation of the tyrosine residue. The differences in the conformation adopted around the two tyrosines of the ITAM motif suggest that they may play different roles pertaining to either binding signal transducing proteins or, alternatively, proteins involved in other processes such as endoplasmic reticulum location. © 1997 John Wiley & Sons, Inc. Biopoly 42: 75–88, 1997

Random coil

Helix (gastropod)

Residue (chemistry)

Coiled coil

Side chain

Motif (music)

Turn (biochemistry)

10.1002/(sici)1097-0282(199707)42:1<75::aid-bip7>3.3.co;2-s

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Citations (0)

-arrestin-1 mediates the TCR-triggered re-routing of distal receptors to the immunological synapse by a PKC-mediated mechanism

The EMBO Journal (2014)

Elena Fernández‐Arenas E. Calleja Nadia Martinez-Martín Severine Gharbi Rosana Navajas

Immunological synapse

Internalization

Arrestin

Crosstalk

10.1002/embj.201386022

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Citations (40)

TCR Engagement Induces Proline-Rich Tyrosine Kinase-2 (Pyk2) Translocation to the T Cell-APC Interface Independently of Pyk2 Activity and in an Immunoreceptor Tyrosine-Based Activation Motif-Mediated Fashion

The Journal of Immunology (2002)

David Sancho Marı́a C. Montoya Alicia Monjas Mónica Gordón‐Alonso Takuya Katagiri

Abstract The relocation of kinases in T lymphocytes during their cognate interaction with APCs is essential for lymphocyte activation. We found that the proline-rich tyrosine kinase-2 (Pyk2) is rapidly translocated to the T cell-APC contact area upon T cell-specific recognition of superantigen-pulsed APCs. Stimulation with anti-CD3-coated latex microspheres was sufficient for Pyk2 reorientation, and the coengagement of CD28 boosted Pyk2 redistribution. Nevertheless, Pyk2 translocation did not result in its recruitment to lipid rafts. Two results support that Pyk2 translocation was independent of its kinase activity. First, Lck activity was required for TCR-induced Pyk2 translocation, but not for TCR-induced Pyk2 activation. Second, a kinase-dead Pyk2 mutant was equally translocated upon TCR triggering. In addition, Lck activity alone was insufficient to induce Pyk2 reorientation and activation, requiring the presence of at least one intact immunoreceptor tyrosine-based activation motif (ITAM). Despite the dependence on functional Lck and on phosphorylated ITAM for Pyk2 translocation, the ITAM-binding tyrosine kinase ζ-associated protein 70 (ZAP-70) was not essential. All these data suggest that, by translocating to the vicinity of the immune synapse, Pyk2 could play an essential role in T cell activation and polarized secretion of cytokines.

Motif (music)

10.4049/jimmunol.169.1.292

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Citations (43)

H-ras and N-ras are dispensable for T-cell development and activation but critical for protective Th1 immunity

Salvador Iborra Manuel Soto Luiz Stark Aroeira Esther Castellano Balbino Alarcón

Thymocyte

Priming (agriculture)

10.1182/blood-2010-10-315770

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Citations (41)

pppA2'p5A' blocks vesicular stomatitis virus replication in intact cells

Journal of Virology (1984)

Balbino Alarcón Harald Bugany Luis Carrasco

pppA2'p5'A blocked the production of infectious vesicular stomatitis virus in HeLa cells. When this compound was present from the beginning of infection, a selective inhibitory effect was observed in viral protein synthesis. Thus, cellular translation was not affected even after 10 h of incubation with this compound, and the bulk of viral proteins was not synthesized. However, this effect was not observed with ATP, GTP, or the core A2'p5'A. The step blocked by pppA2'p5'A is located early during virus infection, but adsorption, entry, and virus uncoating seemed to be unaffected by this compound. Analysis of the antiviral spectrum of pppA2'p5'A indicated that it is active against poliovirus, encephalomyocarditis virus, and Semliki Forest virus and shows no effect against herpes simplex virus type 1 and adenovirus type 5.

Semliki Forest virus

Vesicular Stomatitis

Viral Shedding

Viral Interference

10.1128/jvi.52.1.183-187.1984

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Citations (14)

The CD3-gamma and CD3-delta subunits of the T cell antigen receptor can be expressed within distinct functional TCR/CD3 complexes.

The EMBO Journal (1991)

Balbino Alarcón Steven C. Ley Francisco Sánchez‐Madrid Richard S. Blumberg S T Ju

Delta cell

10.1002/j.1460-2075.1991.tb08023.x

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Citations (98)

Transferrin receptor induces tyrosine phosphorylation in T cells and is physically associated with the TCR zeta-chain.

The Journal of Immunology (1995)

A. Salmerón Aldo Borroto Manuel Fresno Michaël J. Crumpton Steven C. Ley

In addition to being an iron transporter, the transferrin receptor (TfR) has been shown to play a role in T cell activation. Stimulation of the TfR with specific Abs results in T cell proliferation, IL-2 secretion, and protein kinase C activation. In this paper we have analyzed early events caused by activation of the TfR. We have found several protein substrates to be tyrosine phosphorylated upon TfR stimulation in the human Jurkat T cell line. Interestingly, the TfR induced tyrosine phosphorylation in cell lines expressing TCR but not in TCR-negative mutants. Restoration of the TCR surface expression in these mutants reestablished the ability of the TfR to induce tyrosine phosphorylation. This result suggests that activation through the TfR is functionally dependent upon the expression of the TCR. Moreover, the functional relationship of the TfR with the TCR complex is also supported by data showing that TfR stimulation resulted in the tyrosine phosphorylation of the TCR zeta-chain; conversely, stimulation of the TCR complex resulted in an increased tyrosine phosphorylation of the TfR. More importantly, the TfR is shown to associate physically with the TCR zeta-chain as well as with the zeta-binding ZAP70 tyrosine kinase. The TfR/zeta complex is expressed on the cell surface independent of the expression of the other subunits of the TCR complex. We suggest that the TfR/zeta complex is responsible for transducing the TfR-induced signals, and that it could serve to amplify signals delivered by Ag binding to the TCR.

Transferrin receptor

Jurkat cells

10.4049/jimmunol.154.4.1675

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Citations (75)

CCR5 deficiency impairs CD4⁺ T cell memory responses and antigenic sensitivity through increased ceramide synthesis

bioRxiv (Cold Spring Harbor Laboratory) (2020)

Ana Martín‐Leal Raquel Blanco Josefina Casas María Eugenia Sáez Elena Rodríguez‐Bovolenta

ABSTRACT In CD4 + T cells, CCR5 is not only a coreceptor for HIV-1 infection, but also contributes to their functional fitness. Here we show that by limiting GATA-1-induced transcription of specific ceramide synthases, CCR5 signaling reduces ceramide levels and thereby increases T cell antigen receptor (TCR) nanoclustering in antigen-experienced mouse and human CD4 + T cells. This activity is CCR5-specific and independent of CCR5 costimulatory activity. CCR5-deficient mice showed reduced production of high affinity class-switched antibodies, but only after antigen rechallenge, which implies an impaired memory CD4 + T cell response. This study identifies a CCR5 function in the generation of CD4 + T cell memory responses, and establishes an antigen-independent mechanism that regulates TCR nanoclustering by altering specific lipid species.

10.1101/2020.02.14.948893

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Citations (1)

TCR Nanoclusters as the Framework for Transmission of Conformational Changes and Cooperativity

Frontiers in Immunology (2012)

Raquel Blanco Balbino Alarcón

Increasing evidence favors the notion that, before triggering, the T cell antigen receptor (TCR) forms nanometer-scale oligomers that are called nanoclusters. The organization of the TCR in pre-existing oligomers cannot be ignored when analyzing the properties of ligand (pMHC) recognition and signal transduction. As with other membrane receptors, the existence of TCR oligomers points out to cooperativity phenomena. We review the data in support of conformational changes in the TCR as the basic principle to transduce the activation signal to the cytoplasm and the incipient data suggesting cooperativity within nanoclusters.

Cooperativity

Nanoclusters

10.3389/fimmu.2012.00115

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Citations (19)

Role of chimaerins, a group of Rac-specific GTPase activating proteins, in T-cell receptor signaling

Cellular Signalling (2008)

Marı́a J. Caloca Pilar Delgado Balbino Alarcón Xosé R. Bustelo

Immunological synapse

Small GTPase

10.1016/j.cellsig.2007.12.015

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Citations (30)

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