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Article

PKC isoforms activate LRRK1 kinase by phosphorylating conserved residues (Ser1064, Ser1074 and Thr1075) within the CORB GTPase domain.

The Biochemical journal - 30 Sept 2022

Malik Asad U, Karapetsas Athanasios, Nirujogi Raja S, Chatterjee Deep, Phung Toan K, Wightman Melanie, Gourlay Robert, Morrice Nick, Mathea Sebastian, Knapp Stefan, Alessi Dario R

Abstract excerpt

Leucine-rich-repeat-kinase 1 (LRRK1) and its homolog LRRK2 are multidomain kinases possessing a ROC-CORA-CORB containing GTPase domain and phosphorylate distinct Rab proteins. LRRK1 loss of function mutations cause the bone disorder osteosclerotic metaphyseal dysplasia, whereas LRRK2 missense mutations that enhance kinase activity cause Parkinson's disease. Previous work suggested that LRRK1 but not LRRK2, is...

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Identifiers

PMID: 36040231
DOI: 10.1042/BCJ20220308
PMCID: PMC9555798

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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PKC isoforms activate LRRK1 kinase by phosphorylating conserved residues (Ser1064, Ser1074 and Thr1075) within the CORB GTPase domain.PMID 36040231Read ↗

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