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Mechanotransduction Mechanisms of Hypertrophy and Performance with Resistance Exercise
Published in Peter M. Tiidus, Rebecca E. K. MacPherson, Paul J. LeBlanc, Andrea R. Josse, The Routledge Handbook on Biochemistry of Exercise, 2020
Andrew C. Fry, Justin X. Nicoll, Luke A. Olsen
The family of integrin proteins, 24 in all, are heterodimeric consisting of 18 α and 8 β subunits (13). As transmembrane proteins, the integrin physically connects the extracellular matrix to the intracellular space. Within the cell, the integrin indirectly connects to the actin cytoskeleton through scaffolding proteins positioned at the integrin's cytoplasmic tail such as talin, kindlin, and paxillin. Thus, through its transmembrane nature, the integrin allows communication in a bidirectional manner—both in an inside-out and outside-in fashion (96). Interestingly, research has shed light upon the extended physical continuity from the cytoskeleton into the nucleus, made possible by the linker of the nucleoskeleton and cytoskeleton (LINC) complex (109). This continuous physical link from the extracellular space, through the integrin to the cytoskeleton, and into the nucleus via the LINC complex, directly influences gene expression in a matter of seconds upon mechanical activity, such as muscle tension produced with exercise.
Cell Adhesion Molecules in Mast Cell Adhesion and Migration
Published in Bruce S. Bochner, Adhesion Molecules in Allergic Disease, 2020
Harissios Vliagoftis, Dean D. Metcalfe
There are several studies of the phosphorylation of proteins in mast cells after adhesion to extracellular matrix proteins. Adhesion of RBL cells to fibronectin results in the phosphorylation of a 105–115 kD protein (54) that has been shown to be p125FAK (55). Adhesion also results in the phosphorylation of paxillin, but only after FcεRI aggregation (56). Adhesion of BMCMC to vitronectin also induces the phosphorylation of p125FAK. Phosphorylation increases when mast cells are simultaneously activated through FcεRI aggregation. Adhesion of murine mast cells to laminin, and also to the peptide PA22–2 that belongs to the long arm of the A chain of laminin, induces the phosphorylation of a 90–95 kD protein. This protein has not been identified.
Endothelial Cell Signaling During Wound Healing
Published in John J. Lemasters, Constance Oliver, Cell Biology of Trauma, 2020
The activation of FAK may support focal adhesion formation by phosphorylating other cytoskeletal proteins directly. One candidate is the vinculin-binding protein paxillin,85 which is tyrosine phosphorylated during integrin-mediated cell adhesion.68,69 FAK and paxillin colocalize in focal adhesions and have similar tyrosine phosphorylation patterns during development and neuropeptide stimulation.107,108 The phosphotyrosine content of paxillin also correlates with FAK expression in cells that overexpress the focal adhesion kinase.87 This correlation has also been observed for tensin,87 another focal adhesion protein that is tyrosine phosphorylated during integrin-mediated cell-ECM adhesion.109 Tensin is known to contain an SH2 domain,110 and this may facilitate a binding interaction with paxillin or FAK. Finally, a 130-kDa nonkinase phosphoprotein has been described in fibroblasts that is tyrosine phosphorylated during integrin-mediated cell adhesion,111 and may represent another FAK substrate.
Suspended cell lines for inactivated virus vaccine production
Published in Expert Review of Vaccines, 2023
Jiayou Zhang, Zhenyu Qiu, Siya Wang, Zhenbin Liu, Ziling Qiao, Jiamin Wang, Kai Duan, Xuanxuan Nian, Zhongren Ma, Xiaoming Yang
The Src family, also known as the P160 steroid receptor coactivator family, contains three members: Src-1, Src-2, and Src-3. The lack of Src-1 (also known as NCOA1) in human breast cancer cells has been shown to significantly prolong the time of adhesion plaque disassembly and reassembly and reduce the cell adhesion and migration ability on fibronectin [100]. In MCF-7 breast cancer cells, Src-2 knockdown reduced estrogen-induced cell proliferation and target gene expression [114]. Paxillin is a plaque-associated protein involved in regulating integrin signaling and organizing the actin cytoskeleton. Paxillin is associated with many signaling molecules, including adaptor molecules (p130Cas and CRK), kinases (FAK, Pyk2, PAK, and Src), tyrosine phosphatases (PTP – PEST), ARF – GAP proteins (p95pkl and PAG3), and papillomavirus E6 oncoproteins [115]. Paxillin knockout cells have defects in adhesion remodeling [102]; furthermore, loss of Paxillin leads to impaired activation of its downstream target FAK, which is an outward signaling marker of integrin [103].
Serum claudin-5, claudin-11, occludin, vinculin, paxillin, and beta-catenin levels in preschool children with autism spectrum disorder
Published in Nordic Journal of Psychiatry, 2023
Ayhan Bilgiç, Hurşit Ferahkaya, Hülya Karagöz, İbrahim Kılınç, Vesile Meltem Energin
Vinculin and paxillin may be other important molecules for BBB and intestinal barrier functions. Vinculin is a cytoplasmic protein that functions in cell-matrix and cell-cell adhesions and regulation of apoptosis. This molecule also plays a role in the regulation of tight junctions in the intestinal barrier. Like occludin, the research by Vojdani and colleagues found an elevation in antibody production against vinculin in patients with celiac disease and supported its role in intestinal permeability [24]. Paxillin is first defined as a cytoplasmic scaffold/adaptor protein that plays a crucial role in focal adhesion. However, further studies demonstrate that it could also have functions in cell migration, proliferation, and as a regulator of mRNA trafficking and subsequent translation [28]. Therefore, as well as their potential effects on barrier structures, these two molecules contribute to the development of ASD by affecting many developmental and physiological processes.
Advances in the proteomic profiling of the matrisome and adhesome
Published in Expert Review of Proteomics, 2021
The BioID approach has been greatly expanded in a recent study where 16 commonly identified adhesome components were used as baits to decipher the architecture of IACs by MS-based analysis of proteins interacting with individual baits [114]. By combining data from all 16 proteomic datasets, the authors constructed a network of 147 adhesome proteins with 361 interactions. Bioinformatic analysis of the constructed network revealed five protein-protein interaction clusters with a central cluster encompassing the protein paxillin which serves as a critical link with all the other clusters. By contrast, peripheral clusters shared only a small number of direct interactions. The structure and composition of these five clusters overlap with the recent topological models of IAC obtained by imaging experiments [115–117] and likely serve as functional units with specific roles within the complexes.