Abstract
Lemur Tyrosine Kinase 2 (LMTK2) is a recently cloned transmembrane protein, actually a serine/threonine kinase named after the Madagascar primate lemur due to the long intracellular C-terminal tail. LMTK2 is relatively little known, compared to other kinases but its role has been increasingly recognized. Published data show that LMTK2 regulates key cellular events, including endocytic trafficking, nerve growth factor signaling, apoptosis, and Cl− transport. Abnormalities in the expression and function of LMTK2 are associated with human disease, such as neurodegeneration, cancer and infertility. We summarized the current state of knowledge on LMTK2 structure, regulation, interactome, intracellular localization, and tissue expression and point out future research directions to better understand the role of LMTK2.
Highlights
Protein phosphorylation is an important post-translational modification regulating protein– protein interactions and signal transduction (Manning et al, 2002a; Ubersax and Ferrell, 2007; Ardito et al, 2017)
Studies conducted in Chinese hamster ovary (CHO) cells, HeLa cells and in cultured rat cortical neurons demonstrated that phosphorylation of Lemur Tyrosine Kinase 2 (LMTK2) on the S1418 residue, in mouse sequence, activates the kinase (Manser et al, 2012b)
LMTK2 is still incompletely characterized, its role in key biological functions has been well established by strong scientific evidence
Summary
Protein phosphorylation is an important post-translational modification regulating protein– protein interactions and signal transduction (Manning et al, 2002a; Ubersax and Ferrell, 2007; Ardito et al, 2017). Lemur Tyrosine Kinase 2 is composed of 1503 amino acid residues forming a short soluble N-terminal domain, followed by two hydrophobic transmembrane helices (residues 11–29 and 46–63), and a kinase domain (residues 137–407) with the ATP binding site (residues 143–168) (Wang and Brautigan, 2002; Nixon et al, 2013) (Figure 1). The peptide microarray demonstrated that LMTK2 phosphorylates serine and threonine residues preceded or followed by proline (P) residues (Wang and Brautigan, 2006), suggesting similarity with proline-directed kinases. The C-terminal domain is rich in proline residues conforming
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