Matching DNN Compression and Cooperative Training with Resources and Data Availability

To make machine learning (ML) sustainable and apt to run on the diverse devices where relevant data is, it is essential to compress ML models as needed, while still meeting the required learning quality and time performance. However, how much and when an ML model should be compressed, and where its training should be executed, are hard decisions to make, as they depend on the model itself, the resources of the available nodes, and the data such nodes own. Existing studies focus on each of those aspects individually, however, they do not account for how such decisions can be made jointly and adapted to one another. In this work, we model the network system focusing on the training of DNNs, formalize the above multi-dimensional problem, and, given its NP-hardness, formulate an approximate dynamic programming problem that we solve through the PACT algorithmic framework. Importantly, PACT leverages a time- expanded graph representing the learning process, and a data- driven and theoretical approach for the prediction of the loss evolution to be expected as a consequence of training decisions. We prove that PACT’s solutions can get as close to the optimum as desired, at the cost of an increased time complexity, and that, in any case, such complexity is polynomial. Numerical results also show that, even under the most disadvantageous settings, PACT outperforms state-of-the-art alternatives and closely matches the optimal energy cos

Dysfunction of the ciliary ARMC9/TOGARAM1 protein module causes Joubert syndrome

Contains fulltext : 225431.pdf (Publisher’s version ) (Closed access)Joubert syndrome (JBTS) is a recessive neurodevelopmental ciliopathy characterized by a pathognomonic hindbrain malformation. All known JBTS genes encode proteins involved in the structure or function of primary cilia, ubiquitous antenna-like organelles essential for cellular signal transduction. Here, we used the recently identified JBTS-associated protein armadillo repeat motif-containing 9 (ARMC9) in tandem-affinity purification and yeast 2-hybrid screens to identify a ciliary module whose dysfunction underlies JBTS. In addition to the known JBTS-associated proteins CEP104 and CSPP1, we identified coiled-coil domain containing 66 (CCDC66) and TOG array regulator of axonemal microtubules 1 (TOGARAM1) as ARMC9 interaction partners. We found that TOGARAM1 variants cause JBTS and disrupt TOGARAM1 interaction with ARMC9. Using a combination of protein interaction analyses, characterization of patient-derived fibroblasts, and analysis of CRISPR/Cas9-engineered zebrafish and hTERT-RPE1 cells, we demonstrated that dysfunction of ARMC9 or TOGARAM1 resulted in short cilia with decreased axonemal acetylation and polyglutamylation, but relatively intact transition zone function. Aberrant serum-induced ciliary resorption and cold-induced depolymerization in ARMC9 and TOGARAM1 patient cell lines suggest a role for this new JBTS-associated protein module in ciliary stability

Dysfunction of the ciliary ARMC9/TOGARAM1 protein module causes Joubert syndrome

Joubert syndrome (JBTS) is a recessive neurodevelopmental ciliopathy, characterized by a pathognomonic hindbrain malformation. All known JBTS-genes encode proteins involved in the structure or function of primary cilia, ubiquitous antenna-like organelles essential for cellular signal transduction. Here, we use the recently identified JBTS-associated protein ARMC9 in tandem-affinity purification and yeast two-hybrid screens to identify a novel ciliary module whose dysfunction underlies JBTS. In addition to known JBTS-associated proteins CEP104 and CSPP1, we identify CCDC66 and TOGARAM1 as ARMC9 interaction partners. We show that TOGARAM1 variants cause JBTS and disrupt TOGARAM1 interaction with ARMC9. Using a combination of protein interaction analyses and characterization of patient-derived fibroblasts, CRISPR/Cas9-engineered zebrafish and hTERT-RPE1 cells, we demonstrate that dysfunction of ARMC9 or TOGARAM1 results in short cilia with decreased axonemal acetylation and polyglutamylation, but relatively intact transition zone function. Aberrant cold- and serum-induced ciliary loss in both ARMC9 and TOGARAM1 patient cell lines suggests a role for this new JBTS-associated protein module in ciliary stability