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LRRK2 phospho S935

Domain

The seven-bladed WD repeat region is critical for synaptic vesicle trafficking and mediates interaction with multiple vesicle-associated presynaptic proteins (PubMed:24687852). It also mediates homodimerization and regulates kinase activity (PubMed:30635421).

The COR domain mediates homodimerization; it also mediates homotetramerization via interaction with the protein kinase domain.

The Roc domain mediates homodimerization and regulates kinase activity.

Function

The protein expressed by the gene LRRK2 is a serine/threonine-protein kinase that phosphorylates a wide range of proteins involved in neuronal plasticity, autophagy, and vesicle trafficking. It serves as a key regulator of RAB GTPases by affecting the GTP/GDP exchange and interaction partners of RABs through phosphorylation, targeting proteins like RAB3A, RAB3B, and others. LRRK2 manages the GDP/GTP exchange for RAB8A by phosphorylating 'Thr-72', inhibiting RAB8A's interaction with GDI1/GDI2, and influencing primary ciliogenesis to enhance SHH signaling in the brain. It works with RAB29 in retromer-dependent recycling of proteins between lysosomes and the Golgi. The protein is involved in shaping neuronal morphology in the CNS, synaptic vesicle trafficking, and recruiting SEC16A to assist in ER to Golgi transport. It enhances autophagy via the CaMKK/AMPK pathway and relates to nicotinic acid adenine dinucleotide phosphate receptors and lysosomal activity. LRRK2 phosphorylates PRDX3 and APP, influencing neuron apoptosis. Independently, it inhibits MAPT degradation, fostering MAPT oligomerization. Additionally, LRRK2 possesses GTPase activity that regulates its kinase activity. This supplementary information is collated from multiple sources and compiled automatically.

Involvement in disease

Parkinson disease 8

PARK8

A slowly progressive neurodegenerative disorder characterized by bradykinesia, rigidity, resting tremor, postural instability, neuronal loss in the substantia nigra, and the presence of neurofibrillary MAPT (tau)-positive and Lewy bodies in some patients.

None

The disease is caused by variants affecting the gene represented in this entry.

Post-translational modifications

Autophosphorylated at Ser-1292; autophosphorylation is stimulated by RAB29 (PubMed:28202711, PubMed:28720718, PubMed:29127255, PubMed:29212815, PubMed:30635421, PubMed:38127736). Phosphorylation of Ser-910 and either Ser-935 or Ser-1444 facilitates interaction with YWHAG (PubMed:28202711). Phosphorylation of Ser-910 and/or Ser-935 facilitates interaction with SFN (PubMed:28202711).

Ubiquitinated by TRIM1; undergoes 'Lys-48'-linked polyubiquitination leading to proteasomal degradation.

Sequence similarities

Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family.

Tissue specificity

Expressed in pyramidal neurons in all cortical laminae of the visual cortex, in neurons of the substantia nigra pars compacta and caudate putamen (at protein level). Expressed in neutrophils (at protein level) (PubMed:29127255). Expressed in the brain. Expressed throughout the adult brain, but at a lower level than in heart and liver. Also expressed in placenta, lung, skeletal muscle, kidney and pancreas. In the brain, expressed in the cerebellum, cerebral cortex, medulla, spinal cord occipital pole, frontal lobe, temporal lobe and putamen. Expression is particularly high in brain dopaminoceptive areas.

Cellular localization

  • Cytoplasmic vesicle
  • Perikaryon
  • Golgi apparatus membrane
  • Peripheral membrane protein
  • Cell projection
  • Axon
  • Cell projection
  • Dendrite
  • Endoplasmic reticulum membrane
  • Peripheral membrane protein
  • Cytoplasmic vesicle
  • Secretory vesicle
  • Synaptic vesicle membrane
  • Endosome
  • Lysosome
  • Mitochondrion outer membrane
  • Peripheral membrane protein
  • Cytoplasm
  • Cytoskeleton
  • Cytoplasmic vesicle
  • Phagosome
  • Colocalized with RAB29 along tubular structures emerging from Golgi apparatus (PubMed:23395371, PubMed:38127736). Localizes to endoplasmic reticulum exit sites (ERES), also known as transitional endoplasmic reticulum (tER) (PubMed:25201882). Detected on phagosomes and stressed lysosomes but not detected on autophagosomes induced by starvation (By similarity). Recruitment to stressed lysosomes is dependent on the ATG8 conjugation system composed of ATG5, ATG12 and ATG16L1 and leads to lysosomal stress-induced activation of LRRK2 (By similarity).

Alternative names

PARK8, LRRK2, Leucine-rich repeat serine/threonine-protein kinase 2, Dardarin

Target type

Proteins

Primary research area

Immunology & Infectious Disease

Molecular weight

286103Da

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Search our catalogue for 'LRRK2 phospho S935' (3)

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