Discovering ITGB1BP1 Variant 2: A Potential Drug Target Or Biomarker

Target Name: ITGB1BP1

NCBI ID: G9270

Discovering ITGB1BP1 Variant 2: A Potential Drug Target Or Biomarker

ITGB1BP1 (Integrin-尾1,尾1-padding), also known as ITGB1BP1 variant 2, is a protein that is expressed in the endothelial cells of the body. This protein plays a crucial role in cell-cell adhesion and has been implicated in various diseases , including cancer. The ITGB1BP1 gene has been extensively studied, and several variants of this gene have been identified. This article will focus on the ITGB1BP1 variant 2, which has been shown to be a potential drug target or biomarker.

background

ITGB1BP1 (Integrin-尾1, 尾1-filled), also known as ITGB1BP1 variant 2, is a protein expressed by endothelial cells in the body. This protein plays an important role in cell-cell attachment and various diseases, including cancer. The ITGB1BP1 gene has been extensively studied and multiple variants have been discovered. This article will focus on ITGB1BP1 variant 2, which is a known drug target or biomarker.

Structure of ITGB1BP1 molecule

The ITGB1BP1 molecule belongs to the Integrin 尾1 family, which includes 伪, 尾 and 纬 subfamilies. ITGB1BP1 belongs to the 尾1 family, its coding region consists of 198 amino acids, and its molecular weight is 21.9 kDa. The N-terminal end of the ITGB1BP1 molecule contains a lysine residue, which is involved in the recognition process of binding to integrins.

Discovery of ITGB1BP1 variant 2

The discovery of ITGB1BP1 variant 2 originated from the study of ITGB1BP1 gene mutations. The study found that there is a dominant mutation in the ITGB1BP1 gene, which results in an amino acid substitution. The ITGB1BP1 variant 2 mutation results in an amino acid substitution, from phenylalanine to lysine.

Function of ITGB1BP1 variant 2

ITGB1BP1 variant 2 exerts multiple biological functions in cell biology. In cell-cell attachment, ITGB1BP1 variant 2 is the ligand for integrins to bind to receptors on the cell membrane. In tumorigenesis, ITGB1BP1 variant 2 is closely related to cell adhesion, invasion and metastasis. In addition, ITGB1BP1 variant 2 is also closely related to biological processes such as apoptosis, cell cycle and signal transduction.

Pharmacological significance of ITGB1BP1 variant 2

As a drug target or biomarker, ITGB1BP1 variant 2 has broad application prospects in drug development and disease treatment. Currently, several studies explore ITGB1BP1 variant 2 as a drug target for cancer treatment. For example, studies have found that inhibiting ITGB1BP1 variant 2 can significantly inhibit the invasion and metastasis of breast cancer in mice. In addition, ITGB1BP1 variant 2 can also be used as an indicator of tumor cell metabolic activity, and by monitoring its expression level, it can provide guidance for personalized treatment of tumor patients.

in conclusion

ITGB1BP1 variant 2 is an important molecule with multiple biological functions. As a drug target or biomarker, it has broad application prospects in drug development and disease treatment. Future studies will continue to explore the role of ITGB1BP1 variant 2 in cancer treatment and provide more evidence for the clinical application of ITGB1BP1 variant 2 as a drug target or biomarker.

Protein Name: Integrin Subunit Beta 1 Binding Protein 1

Functions: Key regulator of the integrin-mediated cell-matrix interaction signaling by binding to the ITGB1 cytoplasmic tail and preventing the activation of integrin alpha-5/beta-1 (heterodimer of ITGA5 and ITGB1) by talin or FERMT1. Plays a role in cell proliferation, differentiation, spreading, adhesion and migration in the context of mineralization and bone development and angiogenesis. Stimulates cellular proliferation in a fibronectin-dependent manner. Involved in the regulation of beta-1 integrin-containing focal adhesion (FA) site dynamics by controlling its assembly rate during cell adhesion; inhibits beta-1 integrin clustering within FA by directly competing with talin TLN1, and hence stimulates osteoblast spreading and migration in a fibronectin- and/or collagen-dependent manner. Acts as a guanine nucleotide dissociation inhibitor (GDI) by regulating Rho family GTPases during integrin-mediated cell matrix adhesion; reduces the level of active GTP-bound form of both CDC42 and RAC1 GTPases upon cell adhesion to fibronectin. Stimulates the release of active CDC42 from the membranes to maintain it in an inactive cytoplasmic pool. Participates in the translocation of the Rho-associated protein kinase ROCK1 to membrane ruffles at cell leading edges of the cell membrane, leading to an increase of myoblast cell migration on laminin. Plays a role in bone mineralization at a late stage of osteoblast differentiation; modulates the dynamic formation of focal adhesions into fibrillar adhesions, which are adhesive structures responsible for fibronectin deposition and fibrillogenesis. Plays a role in blood vessel development; acts as a negative regulator of angiogenesis by attenuating endothelial cell proliferation and migration, lumen formation and sprouting angiogenesis by promoting AKT phosphorylation and inhibiting ERK1/2 phosphorylation through activation of the Notch signaling pathway. Promotes transcriptional activity of the MYC promoter

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