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Ades. These signaling cascades translate information from cell surface receptors into
This knowledge would also facilitate the therapeutic modulation of signal transduction pathways in these cells.Introduction SN-38Purity & Documentation adaptor proteins play a essential role in organizing signalosomes, that are molecular complexes involved in signal transduction. These signaling cascades translate details from cell surface receptors into cellular responses. We focused our analysis around the adapter molecule ADAP (adhesion and degranulation promoting adapter protein). To investigate the function of ADAP in immune cells we made use of a genetically engineered mouse lacking this molecule. It‘s known that ADAP plays a part in integrin-mediated signaling pathways top to adhesion and motility in T lymphocytes. Nonetheless, tiny is recognized concerning the part of ADAP in dendritic cells, a specific cell population within the immune program linking the innate and also the adaptive immunity. Using their lengthy dendrites, these cells capture and process antigen material and present it to other immune cells. Here, we give evidence that most dendritic cell functions will not be affected by the lack of ADAP. Interestingly, ADAP-deficient dendritic cells* Correspondence: annegret.reinhold@med.ovgu.de 1 Institute for Molecular and Clinical Immunology, Otto von Guericke University Magdeburg, Leipziger Strasse 44, 39120 Magdeburg, Germany Full list of author facts is obtainable in the end with the articleshowed defects in integrin-mediated cellular responses. These findings have significant implications for the understanding from the function of ADAP in integrin-mediated signaling cascades in dendritic cells. This knowledge would also facilitate the therapeutic modulation of signal transduction pathways in these cells.Introduction Adaptor proteins play a important part in organizing signalosomes, which are molecular complexes involved in signal transduction. Adaptor proteins are subdivided into membrane-anchored adaptor molecules (transmembrane adaptor molecules) and cytosolic adaptor molecules [1]. ADAP (adhesion and degranulation promoting adaptor protein, previously designated PubMed ID:http://www.ncbi.nlm.nih.gov/pubmed/27385778 SLAP-130 or Fyb) is often a cytosolic adaptor molecule expressed by T cells, natural killer (NK) cells, myeloid cells and platelets [2,3]. ADAP is expressed through the early stages of B cell development within the bone marrow, but not in mature B cells [4]. On the structural level, ADAP consists of a one of a kind Nterminal area, a proline-rich area, multiple tyrosinebased signaling motifs, two SH3 domains, two putative?2012 Togni et al.; licensee BioMed Central Ltd. This is an Open Access post distributed under the terms on the Inventive Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, offered the original operate is adequately cited.Togni et al. Cell Communication and Signaling 2012, 10:14 http://www.biosignaling.com/content/10/1/Page 2 ofnuclear localisation internet sites, and an Ena-Vasp homology (EVH1) domain binding website [2,3]. The adapter molecule SKAP55 (expressed by T cells) as well as the ubiquitously expressed homolog SKAP-HOM constitutively bind PubMed ID:https://www.ncbi.nlm.nih.gov/pubmed/28300835 to ADAP. This interaction is predominantly mediated by the proline-rich region of ADAP along with the SH3 domain of SKAP55/SKAP-HOM [5]. Disruption with the ADAPSKAP55 module in T cells impairs conjugate formation involving T cells and antigen-presenting cells (APCs), and lymphocyte-function-associated antigen-1 (LFA-1)mediated adhesion [6,7].
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