Substrate for the leucine-rich repeat kinase 2 (LRRK2) with phosphorylated threonine residue
See full description
Esteves et al (2014) LRRK2, a puzzling protein: Insights into Parkinson's disease pathogenesis. Exp. Neurol. 261 206 PMID: 24907399
Jaleel et al (2007) LRRK2 phosphorylates moesin at threonine-558: characterization of how Parkinson's disease mutants affect kinase activity. Biochem. J. 405(2) 307 PMID: 17447891
LRRKtide (also called moesin) is a peptide substrate for leucine-rich repeat kinase 2 (LRRK2). The sequence of LRRKtide has been derived from the ERM proteins: Ezrin (amino acids 561-573), radixin (amino acids 558-570) and moesin (amino acids 539-553). These proteins influence cytoskeletal dynamics by anchoring the cytoskeleton to the plasma membrane. LRRK2 phosphorylates LRRKtide at its Thr558 site. This peptide contains the phosphorylated threonine residue.
LRRK2 is a large, ubiquitous protein of unknown function. LRRK2 has GTPase and kinase activity, and is located in multiple areas of the cell, associated with intracellular membranes and vesicular structures; suggesting LRRK2 may be involved in several cellular pathways. LRRK2 is also found in most organs and mutations in LRRK2 have been identified in Parkinson’s disease.
The threonine residue at position 9 of this peptide has been phosphorylated.
Search our datasheets by catalogue number, peptide sequence or name.
Discover more about how we can support you and our products.
Find answers to common queries about our products and company.
Cambridge Research Biochemicals 17-18 Belasis Court, Belasis Hall Technology Park Billingham TS23 4AZ
t +44 01642 567 183