LRRK2: Difference between revisions
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== LRRK2 == | == LRRK2 == | ||
<p>This multidomain protein called '''LRRK2''' or '''dardarin''' or '''leucine-rich repeat serine/threonine-protein kinase 2''' is a product of LRRK2 gene. Its abbreviation stands for leucine rich repeat kinase 2 and it belongs to ROCO protein family. Although its precise function is unknown, it is proposed that LRRK2 interacts with microtubules, phosphorylates Rab GTPase which marks membranous cargos moving along the microtubules, phosphorylates β-tubulin, moesin, FoxO1, tau, and others <ref>PMID:24725412</ref>. | <p>This multidomain protein called '''LRRK2''' or '''dardarin''' or '''leucine-rich repeat serine/threonine-protein kinase 2''' is a product of LRRK2 gene. Its abbreviation stands for leucine rich repeat kinase 2 and it belongs to ROCO protein family (see also [[Serine/threonine protein kinase]]). Although its precise function is unknown, it is proposed that LRRK2 interacts with microtubules, phosphorylates Rab GTPase which marks membranous cargos moving along the microtubules, phosphorylates β-tubulin, moesin, FoxO1, tau, and others <ref>PMID:24725412</ref>. The cargo might be implicated in pathology of Parkinson´s disease <ref>PMID: 27830778</ref>.</p> | ||
<p>LRRK2 is 2527 amino acids long protein in which we can distinguish N-terminus with scaffold domains such as armadillo, ankyrin, and leucin-rich repeats interaction motifs, and C-terminus with Ras-like GTPase (ROC domain controlling kinase activity of LRRK2), MAPKKK-like kinase domain, COR domain important for dimerization, and scaffold WD40 domain<ref>PMID: 32814344</ref>. LRRK2 has both GTPase and kinase activity, mediated by ROC domain and kinase domain, respectively, and the kinase activity is regulated by the ROC domain <ref name="sest">PMID: 17706965</ref>.</p> | <p>LRRK2 is 2527 amino acids long protein in which we can distinguish N-terminus with scaffold domains such as armadillo, ankyrin, and leucin-rich repeats interaction motifs, and C-terminus with Ras-like GTPase (ROC domain controlling kinase activity of LRRK2), MAPKKK-like kinase domain, COR domain important for dimerization, and scaffold WD40 domain<ref>PMID: 32814344</ref>. LRRK2 has both GTPase and kinase activity, mediated by ROC domain and kinase domain, respectively, and the kinase activity is regulated by the ROC domain <ref name="sest">PMID: 17706965</ref>.</p> | ||
<p>COR domain represents a central part in head-to-head orientation when LRRK2 folds into predominant form of globular dimer, where kinase-WD40 modul folds back to domains of N-terminus and thus allows these parts to interact and create autophosphorylation sites <ref name="guaitoli"/>.</p> | <p>COR domain represents a central part in head-to-head orientation when LRRK2 folds into predominant form of globular dimer, where kinase-WD40 modul folds back to domains of N-terminus and thus allows these parts to interact and create autophosphorylation sites <ref name="guaitoli"/>.</p> | ||
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On top of that, the R1441C mutation has also been shown to improve binding of LRRK2 to neuronal microtubules <ref>PMID: 22080837</ref>.</p> | On top of that, the R1441C mutation has also been shown to improve binding of LRRK2 to neuronal microtubules <ref>PMID: 22080837</ref>.</p> | ||
==3D structures of LRRK2== | |||
[[LRRK2 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||