Mitogen-activated protein kinase 14 (MAPK14), Proto-oncogene tyrosine-protein kinase Src (SRC), Heat shock protein HSP 90-alpha (HSP90AA1), and Matrix metalloproteinase-9 (MMP9) (MAPK14, SRC, HSP90AA1, MMP9)

This target entry represents a multi-protein profile consisting of Mitogen-activated protein kinase 14 (MAPK14), Proto-oncogene tyrosine-protein kinase Src (SRC), Heat shock protein HSP 90-alpha (HSP90AA1), and Matrix metalloproteinase-9 (MMP9). MAPK14, also known as p38 alpha, is a key mediator of cellular responses to external stimuli such as cytokines and stress, playing a significant role in inflammation (UniProt Q16539). SRC is a non-receptor tyrosine kinase involved in signaling pathways that control cell proliferation, survival, and migration, and is frequently implicated in cancer progression (UniProt P12931). HSP90AA1 is a molecular chaperone that assists in the folding and stabilization of various proteins, particularly those involved in signal transduction and cell cycle progression (UniProt P07900). MMP9 is an enzyme that breaks down extracellular matrix components, which is crucial for processes like wound healing and tumor metastasis (UniProt P14780). Together, these four proteins are often analyzed as a network in systems biology or multi-target drug discovery efforts aimed at complex diseases like cancer and chronic inflammation. Drugs targeting these molecules range from kinase inhibitors like dasatinib to chaperone inhibitors like tanespimycin, each addressing different nodes of the cellular signaling and structural network.

Other names

p38-alphaSAPK2ACSBPc-Srcpp60c-srcASVHSP90AHSPC1HSPCAGelatinase B92 kDa type IV collagenaseCLG4B

The mechanism of action involves the inhibition of specific enzymatic or chaperone activities: MAPK14 and SRC are targeted by ATP-competitive kinase inhibitors; HSP90AA1 is targeted by inhibitors that bind its N-terminal ATP-binding domain, leading to the degradation of oncogenic client proteins; and MMP9 is targeted by inhibitors that block its catalytic activity, often by chelating the essential zinc ion (UniProt Q16539, P12931, P07900, P14780).