Calcium-and integrin-binding protein 1(CIB1),a member of calcium binding protein containing EF-hand domain,has been shown to bind a variety of signaling proteins. Interaction of CIB1 with its various binding partners provides valuable insight into potential mechanisms by which CIB1 may regulate diverse tumors characteristic biological process that range from adhesion,migration,cell survival,proliferation,and angiogenesis. CIB1 has also been implicated in both the increase and decrease of cell proliferation.CIB1 promoted cell proliferation and survival by adjusted tumor-associated extracellular regulated protein kinases 1/2(ERK1/2),phosphatidylinositol 3 kinase(PI-3K)/v-akt murine thymoma viral oncogene homolog-dependent signaling pathway,or increased cell migration by activating Src family kinases,protein kinase C,PI-3K,and ERK 1/2-mediated signaling pathway.CIB1 inhibited cell proliferation through inhibiting polo-like kinases 3(PLK3) activity.It also inhibits cell migration by binding to and activating p21-activated kinase 1. Especially a large subset of triple-negative breast cancer may display non-oncogene addiction to CIB1,a phenomenon in which cancer cells require,or become 'addicted' to a non-mutated,non-overexpressed gene/protein that is nonetheless essential to maintain oncogenic signaling pathways,and implicate CIB1 as a novel drug target in tumors. Additionally,CIB1 plays a role in such pathological processes as cardiac hypertrophy,deafness,and male infertility. Research on CIB1 function has important clinical significance. In this review,we discussed current understanding of CIB1 in human tumors.
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http://dx.doi.org/10.3881/j.issn.1000-503X.2017.05.020 | DOI Listing |
J Dairy Sci
January 2025
Department of Molecular Biology and Genetics, Aarhus University, 8000 Aarhus C, Denmark. Electronic address:
Insufficient absorption of iron and the consequent development of iron deficiency have serious health consequences. Hence, identification and development of iron delivery systems that can increase the bioavailability and uptake of dietary iron are important. Osteopontin (OPN) is an acidic and highly phosphorylated integrin-binding protein found in milk where it exists as a full-length protein and as N-terminally derived fragments.
View Article and Find Full Text PDFInt J Biol Macromol
November 2024
Magnetic Resonance Center, Department of Chemistry, University of Florence, Sesto Fiorentino, Italy. Electronic address:
Calcium- and Integrin-Binding protein 2 (CIB2) is a widely expressed protein with an uncertain biological role. Two of its four EF-hand motifs bind Mg(II) and/or Ca(II), thus triggering conformational changes. Although previous studies suggested that CIB2 preferentially binds Mg(II) over Ca(II) under physiological conditions, an atomic level characterization of CIB2 in the presence of both cations was lacking.
View Article and Find Full Text PDFStem Cell Res
December 2024
Key Laboratory of Combined Multi-organ Transplantation, Ministry of Public Health, the First Affiliated Hospital, Zhejiang University School of Medicine, Hangzhou 310003, China; Institute of Translational Medicine, Zhejiang University, Hangzhou 310029, China. Electronic address:
bioRxiv
August 2024
Laboratory of Cell Structure and Dynamics, National Institute on Deafness and Other Communication Disorders, National Institutes of Health, Bethesda, MD 20892, USA.
Microvilli-membrane bound actin protrusions on the surface of epithelial cells-are sites of critical processes including absorption, secretion, and adhesion. Increasing evidence suggests microvilli are mechanosensitive, but underlying molecules and mechanisms remain unknown. Here, we localize transmembrane channel-like proteins 4 and 5 (TMC4 and 5) and calcium and integrin binding protein 3 (CIB3) to microvillar tips in intestinal epithelial cells, near glycocalyx insertion sites.
View Article and Find Full Text PDFbioRxiv
July 2024
Department of Otorhinolaryngology - Head & Neck Surgery, University of Maryland School of Medicine, Baltimore, MD, USA.
Variations in genes coding for calcium and integrin binding protein 2 (CIB2) and whirlin cause deafness both in humans and mice. We previously reported that CIB2 binds to whirlin, and is essential for normal staircase architecture of auditory hair cells stereocilia. Here, we refine the interacting domains between these proteins and provide evidence that both proteins have distinct role in the development and organization of stereocilia bundles required for auditory transduction.
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