Matches in UGent Biblio for { <https://biblio.ugent.be/publication/5928583#aggregation> ?p ?o. }
Showing items 1 to 47 of
47
with 100 items per page.
- aggregation classification "A1".
- aggregation creator B995187.
- aggregation creator B995188.
- aggregation creator B995189.
- aggregation creator B995190.
- aggregation creator B995191.
- aggregation creator B995192.
- aggregation creator B995193.
- aggregation creator B995194.
- aggregation creator B995195.
- aggregation creator B995196.
- aggregation creator B995197.
- aggregation creator B995198.
- aggregation creator B995199.
- aggregation creator B995200.
- aggregation creator person.
- aggregation creator person.
- aggregation date "2015".
- aggregation format "application/pdf".
- aggregation hasFormat 5928583.bibtex.
- aggregation hasFormat 5928583.csv.
- aggregation hasFormat 5928583.dc.
- aggregation hasFormat 5928583.didl.
- aggregation hasFormat 5928583.doc.
- aggregation hasFormat 5928583.json.
- aggregation hasFormat 5928583.mets.
- aggregation hasFormat 5928583.mods.
- aggregation hasFormat 5928583.rdf.
- aggregation hasFormat 5928583.ris.
- aggregation hasFormat 5928583.txt.
- aggregation hasFormat 5928583.xls.
- aggregation hasFormat 5928583.yaml.
- aggregation isPartOf urn:issn:0021-9533.
- aggregation language "eng".
- aggregation rights "I have transferred the copyright for this publication to the publisher".
- aggregation subject "Biology and Life Sciences".
- aggregation title "LRRK2 functions in synaptic vesicle endocytosis through a kinase-dependent mechanism".
- aggregation abstract "Mutations in leucine-rich repeat kinase 2 (LRRK2) are associated with Parkinson's disease, but the precise physiological function of the protein remains ill-defined. Recently, our group proposed a model in which LRRK2 kinase activity is part of an EndoA phosphorylation cycle that facilitates efficient vesicle formation at synapses in the Drosophila melanogaster neuromuscular junctions. Flies harbor only one Lrrk gene, which might encompass the functions of both mammalian LRRK1 and LRRK2. We therefore studied the role of LRRK2 in mammalian synaptic function and provide evidence that knockout or pharmacological inhibition of LRRK2 results in defects in synaptic vesicle endocytosis, altered synaptic morphology and impairments in neurotransmission. In addition, our data indicate that mammalian endophilin A1 (EndoA1, also known as SH3GL2) is phosphorylated by LRRK2 in vitro at T73 and S75, two residues in the BAR domain. Hence, our results indicate that LRRK2 kinase activity has an important role in the regulation of clathrin-mediated endocytosis of synaptic vesicles and subsequent neurotransmission at the synapse.".
- aggregation authorList BK1400426.
- aggregation endPage "552".
- aggregation issue "3".
- aggregation startPage "541".
- aggregation volume "128".
- aggregation aggregates 5928601.
- aggregation isDescribedBy 5928583.
- aggregation similarTo jcs.158196.
- aggregation similarTo LU-5928583.