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• W2083438412 abstract "Leucine-rich repeat kinase 2 (LRRK2) has been associated with Parkinson's disease (PD) and other disorders. However, its normal physiological functions and pathogenic properties remain elusive. Here we show that LRRK2 regulates the anterograde ER-Golgi transport through anchoring Sec16A at the endoplasmic reticulum exit sites (ERES). LRRK2 interacted and co-localized with Sec16A, a key protein in the formation of ERES. Lrrk2 depletion caused a dispersion of Sec16A from ERES and impaired ER export. In neurons, LRRK2 and Sec16A showed extensive co-localization at the dendritic ERES (dERES) that locally regulate the transport of proteins to the dendritic spines. A loss of Lrrk2 affected the association of Sec16A with dERES and impaired the activity-dependent targeting of glutamate receptors onto the cell/synapse surface. Furthermore, the PD-related LRRK2 R1441C missense mutation in the GTPase domain interfered with the interaction of LRRK2 with Sec16A and also affected ER-Golgi transport, while LRRK2 kinase activity was not required for these functions. Therefore, our findings reveal a new physiological function of LRRK2 in ER-Golgi transport, suggesting ERES dysfunction may contribute to the pathogenesis of PD." @default.
• W2083438412 created "2016-06-24" @default.
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• W2083438412 date "2014-09-08" @default.
• W2083438412 modified "2023-10-02" @default.
• W2083438412 title "Leucine‐rich repeat kinase 2 regulates Sec16A at <scp>ER</scp> exit sites to allow <scp>ER</scp> –Golgi export" @default.
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• W2083438412 doi "https://doi.org/10.15252/embj.201487807" @default.
• W2083438412 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4253522" @default.
• W2083438412 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/25201882" @default.
• W2083438412 hasPublicationYear "2014" @default.
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