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TitleStructure of LRRK1 and mechanisms of autoinhibition and activation.
Journal, issue, pagesNat Struct Mol Biol, Vol. 30, Issue 11, Page 1735-1745, Year 2023
Publish dateOct 19, 2023
AuthorsJanice M Reimer / Andrea M Dickey / Yu Xuan Lin / Robert G Abrisch / Sebastian Mathea / Deep Chatterjee / Elizabeth J Fay / Stefan Knapp / Matthew D Daugherty / Samara L Reck-Peterson / Andres E Leschziner /
PubMed AbstractLeucine Rich Repeat Kinase 1 and 2 (LRRK1 and LRRK2) are homologs in the ROCO family of proteins in humans. Despite their shared domain architecture and involvement in intracellular trafficking, ...Leucine Rich Repeat Kinase 1 and 2 (LRRK1 and LRRK2) are homologs in the ROCO family of proteins in humans. Despite their shared domain architecture and involvement in intracellular trafficking, their disease associations are strikingly different: LRRK2 is involved in familial Parkinson's disease while LRRK1 is linked to bone diseases. Furthermore, Parkinson's disease-linked mutations in LRRK2 are typically autosomal dominant gain-of-function while those in LRRK1 are autosomal recessive loss-of-function. Here, to understand these differences, we solved cryo-EM structures of LRRK1 in its monomeric and dimeric forms. Both differ from the corresponding LRRK2 structures. Unlike LRRK2, which is sterically autoinhibited as a monomer, LRRK1 is sterically autoinhibited in a dimer-dependent manner. LRRK1 has an additional level of autoinhibition that prevents activation of the kinase and is absent in LRRK2. Finally, we place the structural signatures of LRRK1 and LRRK2 in the context of the evolution of the LRRK family of proteins.
External linksNat Struct Mol Biol / PubMed:37857821 / PubMed Central
MethodsEM (single particle)
Resolution3.4 - 4.6 Å
Structure data

27813

8e04

EMDB-27813, PDB-8e04:
Structure of monomeric LRRK1
Method: EM (single particle) / Resolution: 3.8 Å

EMDB-27814: Local refinement around RCKW of LRRK1
Method: EM (single particle) / Resolution: 3.54 Å

EMDB-27815: Local refinement of LRRK1 around the ROC-COR-kinase domains
Method: EM (single particle) / Resolution: 3.7 Å

EMDB-27816: Local refinement around kinase and WD40 domains of LRRK1
Method: EM (single particle) / Resolution: 3.4 Å

27817

8e05

EMDB-27817, PDB-8e05:
Structure of dimeric LRRK1
Method: EM (single particle) / Resolution: 4.6 Å

27818

8e06

EMDB-27818, PDB-8e06:
Symmetry expansion of dimeric LRRK1
Method: EM (single particle) / Resolution: 4.3 Å

Chemicals

ChemComp-GDP:
GUANOSINE-5'-DIPHOSPHATE / GDP, energy-carrying molecule*YM / Guanosine diphosphate

Source
  • homo sapiens (human)
KeywordsTRANSFERASE / monomer / dimer

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