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Arango, A.

Publications and source records attributed to Arango, A..

2 recordsLinked to original sources

Parallel processing of orthogonal manifolds enables zero-shot composition in recurrent networks

Animals flexibly combine learned behaviors into novel actions without practicing their combinations, yet the computational mechanisms that enable independently acquired computations to be expressed in parallel remain unclear. Here we show that feedback geometry during learning determines whether recurrent dynamics can be recombined through zero-shot parallel composition. Using recurrent networks trained by a local predictive plasticity rule, we found that distinct feedback vectors embed independently learned computations in separable dynamical subspaces, allowing novel input combinations to co-activate these components and generate composite outputs without joint training. In contrast, aligned feedback vectors, as well as networks trained by backpropagation through time, exhibited accurate single-task performance but failed to support parallel composition, demonstrating that task acquisition and future reusability are dissociable properties of learning. A combined input evoked a single composite population trajectory, whose projections onto feedback-shaped task subspaces recovered the independently learned component dynamics. The same principle reproduced additive reach-posture geometry observed in motor cortex and generalized to higher-dimensional movement primitives. These results identify feedback geometry as a computational principle by which learning systems structure recurrent dynamics for future compositional reuse.

neuroscience↗

Phosphatidic acid inhibits SNARE priming by inducing conformational changes in Sec18 protomers

Eukaryotic homeostasis relies on membrane fusion catalyzed by SNARE proteins. Inactive SNARE bundles are re-activated by Sec18/NSF driven disassembly to enable a new round of fusion. We previously found that phosphatidic acid (PA) binds Sec18 to sequester it from SNAREs. Dephosphorylation of PA dissociates Sec18 from the membrane allowing it to engage SNARE complexes. We now report that PA induces conformational changes in Sec18 protomers, while hexameric Sec18 cannot bind PA membranes. The association of Sec18 with PA was shown to be sensitive to membrane curvature, suggesting that regulation could vary on different organelles in a curvature dependent manner. Molecular dynamics showed that PA binding sites exist on the D1 and D2 domains of Sec18 and that residues needed for binding were masked in the hexameric form of the protein. Together these data indicate that PA regulates Sec18 function through altering protein architecture and stabilizing membrane-bound protomers.

biochemistry↗