LAMP2A protein levels are regulated post-translationally by the AAA+ ATPase torsinA, which mediates extraction of aged or damaged LAMP2A from the lysosomal membrane for degradation. This torsinA-dependent turnover normally maintains a young pool of LAMP2A with high translocation competence. In PD, SNCA oligomers bind directly to the LAMP2A cytosolic domain (residues 1-24), physically blocking the torsinA recognition motif without affecting LAMP2A's ability to form SNCA complexes. This creates a
Radar Chart — 10 Dimensions
Score Comparison Bars
Mechanistic
0.68
Evidence
0.62
Novelty
0.90
Feasibility
0.00
Impact
0.00
Druggability
0.00
Safety
0.00
Competition
0.00
Data
0.00
Reproducible
0.00
KG Connect
0.19
Score Breakdown
Dimension
SNCA Oligomer Binding to LAMP2
Mechanistic
0.680
Evidence
0.620
Novelty
0.900
Feasibility
0.000
Impact
0.000
Druggability
0.000
Safety
0.000
Competition
0.000
Data
0.000
Reproducible
0.000
KG Connect
0.187
Evidence
SNCA Oligomer Binding to LAMP2A Cytosolic Tail Prevents Tors