Blobby is a synaptic active zone assembly protein required for memory in Drosophila

J. Lützkendorf, T. Matkovic-Rachid, S. Liu, T. Götz, L. Gao, O. Turrel, M. Maglione, M. Grieger, S. Putignano, N. Ramesh, T. Ghelani, A. Neumann, N. Gimber, J. Schmoranzer, A. Stawrakakis, B. Brence, D. Baum, Kai Ludwig, M. Heine, T. Mielke, F. Liu, A. M. Walter, M. C. Wahl and S. J. Sigrist ()
Additional contact information
J. Lützkendorf: Institute for Biology and Genetics
T. Matkovic-Rachid: Institute for Biology and Genetics
S. Liu: Institute of Chemistry and Biochemistry/Structural Biochemistry
T. Götz: Institute for Biology and Genetics
L. Gao: Institute for Biology and Genetics
O. Turrel: Institute for Biology and Genetics
M. Maglione: Institute for Biology and Genetics
M. Grieger: Institute for Biology and Genetics
S. Putignano: Institute for Biology and Genetics
N. Ramesh: Institute for Biology and Genetics
T. Ghelani: Institute for Biology and Genetics
A. Neumann: Institute for Biology and Genetics
N. Gimber: Advanced Medical Bioimaging Core Facility
J. Schmoranzer: Advanced Medical Bioimaging Core Facility
A. Stawrakakis: Institute for Biology and Genetics
B. Brence: Department of Visual and Data-Centric Computing
D. Baum: Department of Visual and Data-Centric Computing
Kai Ludwig: Forschungszentrum für Elektronenmikroskopie
M. Heine: Johannes Gutenberg University Mainz
T. Mielke: Microscopy and Cryo-Electron Microscopy Service Group
F. Liu: Campus Berlin-Buch
A. M. Walter: Campus Berlin-Buch
M. C. Wahl: Institute of Chemistry and Biochemistry/Structural Biochemistry
S. J. Sigrist: Institute for Biology and Genetics

Nature Communications, 2025, vol. 16, issue 1, 1-20

Abstract: Abstract At presynaptic active zones (AZs), scaffold proteins are critical for coordinating synaptic vesicle release and forming essential nanoarchitectures. However, regulatory principles steering AZ scaffold assembly, function, and plasticity remain insufficiently understood. We here identify an additional Drosophila AZ protein, “Blobby”, essential for proper AZ nano-organization. Blobby biochemically associates with the ELKS family AZ scaffold protein Bruchpilot (BRP) and integrates into newly forming AZs. Loss of Blobby results in fewer AZs forming, ectopic AZ scaffold protein accumulations (“blobs”) and disrupts nanoscale architecture of the BRP-AZ scaffold. Functionally, blobby mutants show diminished evoked synaptic currents due to reduced synaptic vesicle release probability and fewer functional release sites. Blobby is also present in adult brain synapses, and post-developmental knockdown of Blobby in the mushroom body impairs olfactory aversive memory consolidation. Thus, our analysis identifies an additional layer of AZ regulation critical for developmental AZ assembly but also for AZ-mediated plasticity controlling behavior.

Date: 2025
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DOI: 10.1038/s41467-024-55382-9

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