MEK5 is a dual specific kinase that specifically activates ERK5 involved in the regulation of diverse cellular processes, including cell growth, survival, and differentiation. The MEK5-ERK5 pathway is activated in numerous cancer types and plays a role in tumor growth and metastasis. Pharmacological targeting of the MEK5-ERK5 pathway has been investigated as a strategy for cancer treatment. MEK5 is activated by a variety of stimuli, including growth factors, cytokines, and oxidative stress. Activation of MEK5 is triggered by upstream kinases MEKK2 and MEKK3, leading to phosphorylation of MEK5 at Ser311 and Thr315, which subsequently leads to MEK5 dependent phosphorylation of EKR5 at Thr218 and Tyr220. Phosphorylation of ERK5 leads to nuclear translocation and regulation of several oncogenic transcription factors, including MEF2C, c-Fos, c-Myc, and Sap1.
The protein encoded by this gene is a dual specificity protein kinase that belongs to the MAP kinase kinase family. This kinase specifically activates MAPK8/JNK1 and MAPK9/JNK2, and this kinase itself is phosphorylated and activated by MAP kinase kinase kinases including MAP3K1/MEKK1, MAP3K2/MEKK2,MAP3K3/MEKK5, and MAP4K2/GCK. This kinase is involved in the signal transduction mediating the cell responses to proinflammatory cytokines, and environmental stresses. Alternative splicing results in multiple transcript variants.
Expression is restricted to melanoma and melanocyte cell lines and retina.
Meprin A subunit alpha, also known as MEP1A, and Endopeptidase-2, is a single-pass type I membrane protein that belongs to the peptidase M12A family. MEP1A contains one EGF-like domain, one MAM domain, and one MATH domain. Meprins are unique plasma membrane and secreted metalloproteinases that are highly regulated at the transcriptional and post-translational levels. Meprin alpha and beta subunits are abundantly expressed in kidney and intestinal epithelial cells, are secreted into the urinary tract and intestinal lumen and are found in leukocytes and cancer cells under certain conditions. Meprins are capable of proteolytically degrading extracellular matrix proteins, processing bioactive proteins, and play a role in inflammatory processes. Meprin A and B are highly regulated, secreted and cell-surface homo- and hetero-oligomeric enzymes. Meprins are abundantly expressed in the kidney and intestine. The multidomain alpha and beta subunits have high sequence identity. They have very different substrate specificities, oligomerization potentials, and are differentially regulated. Meprin A appears to be an important therapeutic target and urinary excretion appears to be a potential biomarker of acute kidney injury ( AKI ).
This gene is a member of the MER/AXL/TYRO3 receptor kinase family and encodes a transmembrane protein with two fibronectin type-III domains, two Ig-like C2-type (immunoglobulin-like) domains, and one tyrosine kinase domain. Mutations in this gene have been associated with disruption of the retinal pigment epithelium (RPE) phagocytosis pathway and onset of autosomal recessive retinitis pigmentosa (RP).
Chaperone specifically assisting the folding of beta-propeller/EGF modules within the family of low-density lipoprotein receptors (LDLRs. Acts as a modulator of the Wnt pathway through chaperoning the coreceptors of the canonical Wnt pathway, LRP5 and LRP6, to the plasma membrane. Essential for specification of embryonic polarity and mesoderm induction. Plays an essential role in neuromuscular junction (NMJ formation by promoting cell-surface expression of LRP4 (By similarity. May regulate phagocytosis of apoptotic retinal pigment epithelium (RPE cells (By similarity.
Membrane-anchored forms may play a role in cellular adhesion. Megakaryocyte-potentiating factor (MPF) potentiates megakaryocyte colony formation in vitro.
Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.,cofactor:Binds 1 sodium ion per subunit. The sodium ion has a structural role.,cofactor:Binds 2 cobalt ions per subunit.,cofactor:Binds 2 cobalt ions per subunit. The true nature of the physiological cofactor is under debate. The enzyme is also active with zinc, manganese or divalent iron ions.,Removes the amino-terminal methionine from nascent proteins.,Removes the amino-terminal methionine from nascent proteins. Required for normal progression through the cell cycle.,similarity:Belongs to the peptidase M24A family.
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