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TitleCapture, mutual inhibition and release mechanism for aPKC-Par6 and its multisite polarity substrate Lgl.
Journal, issue, pagesNat Struct Mol Biol, Vol. 32, Issue 4, Page 729-739, Year 2025
Publish dateJan 6, 2025
AuthorsChristopher P Earl / Mathias Cobbaut / André Barros-Carvalho / Marina E Ivanova / David C Briggs / Eurico Morais-de-Sá / Peter J Parker / Neil Q McDonald /
PubMed AbstractThe mutually antagonistic relationship of atypical protein kinase C (aPKC) and partitioning-defective protein 6 (Par6) with the substrate lethal (2) giant larvae (Lgl) is essential for regulating ...The mutually antagonistic relationship of atypical protein kinase C (aPKC) and partitioning-defective protein 6 (Par6) with the substrate lethal (2) giant larvae (Lgl) is essential for regulating polarity across many cell types. Although aPKC-Par6 phosphorylates Lgl at three serine sites to exclude it from the apical domain, aPKC-Par6 and Lgl paradoxically form a stable kinase-substrate complex, with conflicting roles proposed for Par6. We report the structure of human aPKCι-Par6α bound to full-length Llgl1, captured through an aPKCι docking site and a Par6 contact. This complex traps a phospho-S663 Llgl1 intermediate bridging between aPKC and Par6, impeding phosphorylation progression. Thus, aPKCι is effectively inhibited by Llgl1 while Llgl1 is captured by aPKCι-Par6. Mutational disruption of the Lgl-aPKC interaction impedes complex assembly and Lgl phosphorylation, whereas disrupting the Lgl-Par6 contact promotes complex dissociation and Lgl phosphorylation. We demonstrate a Par6-regulated substrate capture-and-release model requiring binding by active Cdc42 and the apical partner Crumbs to drive complex disassembly. Our results suggest a mechanism for mutual regulation and spatial control of aPKC-Par6 and Lgl activities.
External linksNat Struct Mol Biol / PubMed:39762628 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution2.591 - 3.68 Å
Structure data

18877

8r3y

EMDB-18877, PDB-8r3y:
Cryo EM structure of a stable LGL/aPKC Iota/Par-6 complex
Method: EM (single particle) / Resolution: 3.68 Å

PDB-8r3x:
Crystal structure of aPKC Iota kinase domain with LLGL2 peptide
Method: X-RAY DIFFRACTION / Resolution: 2.591 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-ANP:
PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER / AMP-PNP, energy-carrying molecule analogue*YM

Source
  • homo sapiens (human)
KeywordsCYTOSOLIC PROTEIN / Kinase / Polarity / Kinase substrate complex.

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