SNAP91

Last update 08 May 2025

Basic Info

Synonyms

91 kDa synaptosomal-associated protein, AP180, CALM

+ [6]

Introduction

Adaptins are components of the adapter complexes which link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration. Binding of AP180 to clathrin triskelia induces their assembly into 60-70 nm coats (By similarity).

100 Clinical Results associated with SNAP91

100 Translational Medicine associated with SNAP91

0 Patents (Medical) associated with SNAP91

197

Literatures (Medical) associated with SNAP91

01 Apr 2025·Protein Science

Sizes, conformational fluctuations, and SAXS profiles for intrinsically disordered proteins

Article

Author: Mugnai, Mauro L. ; Zeno, Wade ; Stachowiak, Jeanne C. ; Kumar, Abhinaw ; Chakraborty, Debayan ; Nguyen, Hung T. ; Thirumalai, D. ; Straub, John E. ; Maksudov, Farkhad

AbstractThe preponderance of intrinsically disordered proteins (IDPs) in the eukaryotic proteome, and their ability to interact with each other, and with folded proteins, RNA, and DNA for functional purposes, have made it important to quantitatively characterize their biophysical properties. Toward this end, we developed the transferable self‐organized polymer (SOP‐IDP) model to calculate the properties of several IDPs. The values of the radius of gyration () obtained from SOP‐IDP simulations are in excellent agreement (correlation coefficient of 0.96) with those estimated from SAXS experiments. For AP180 and Epsin, the predicted values of the hydrodynamic radii () are in nearly quantitative agreement with those from fluorescence correlation spectroscopy (FCS) experiments. Strikingly, the calculated SAXS profiles for 36 IDPs are also nearly superimposable on the experimental profiles. The dependence of and the mean end‐to‐end distance () on chain length, , follows Flory's scaling law, ( and ), suggesting that globally IDPs behave as synthetic polymers in a good solvent. This finding depends on the solvent quality, which can be altered by changing variables such as pH and salt concentration. The values of and are 0.20 and 0.48 nm, respectively. Surprisingly, finite size corrections to scaling, expected on theoretical grounds, are negligible for and . In contrast, only by accounting for the finite sizes of the IDPs, the dependence of experimentally measurable on can be quantitatively explained using . Although Flory scaling law captures the estimates for , , and accurately, the spread of the simulated data around the theoretical curve is suggestive of of sequence‐specific features that emerge through a fine‐grained analysis of the conformational ensembles using hierarchical clustering. Typically, the ensemble of conformations partitions into three distinct clusters, having different equilibrium populations and structural properties. Without any further readjustments to the parameters of the SOP‐IDP model, we also obtained nearly quantitative agreement with paramagnetic relaxation enhancement (PRE) measurements for α‐synuclein. The transferable SOP‐IDP model sets the stage for several applications, including the study of phase separation in IDPs and interactions with nucleic acids.

01 Apr 2025·Journal of Biological Chemistry

α-Synuclein interacts directly with AP2 and regulates its binding to synaptic membranes

Article

Author: Vargas, Karina J ; Mooney, Ian ; Morgan, Jennifer R ; Owen, David J ; Wallace, Jaqulin N

α-Synuclein mutation and aggregation are associated with several neurodegenerative disorders, including Parkinson's disease, dementia with Lewy bodies and multiple system atrophy. It is expressed in the presynaptic compartment where it regulates clathrin mediated synaptic vesicle endocytosis. We have shown that α-synuclein regulates clathrin lattice size and curvature in vitro. However, the molecular mechanism by which this occurs remains unknown. Here, we show a strong colocalization between the heterotetrametric clathrin adaptor protein-2 (AP2) and α-synuclein at presynapses. Moreover, we report a direct biochemical interaction between the AP2 core domain and the C-terminal domain of α-synuclein. We further show that α-synuclein binds to isolated synaptic membranes in an ATP-dependent manner, similar to AP2 and the monomeric adaptor protein, 180 KDa (AP180), suggesting that α-synuclein, AP2 and AP180 share a common synaptic membrane binding pathway. In contrast, other endocytic proteins, such as clathrin heavy chain and the large GTPase dynamin-1 bind to synaptic membranes independently of ATP. After immunodepleting α-synuclein, we observed a specific reduction in AP2 binding to synaptic membranes, indicating that α-synuclein interaction with AP2 is necessary to maintain normal levels of AP2 on synaptic membranes. These findings demonstrate that α-synuclein plays a critical role in stabilizing AP2 on synaptic membranes, an event which is required for initiation of clathrin-mediated synaptic vesicle endocytosis.

01 Apr 2025·Molecular & Cellular Proteomics

Ca2+-Triggered (de)ubiquitination Events in Synapses

Article

Author: Lorenz, Sonja ; Rizzoli, Silvio O ; Kaufmann, Svenja V ; Urlaub, Henning ; Ainatzi, Sofia ; Georgiev, Svilen V ; Silbern, Ivan

Neuronal communication relies on neurotransmitter release from synaptic vesicles (SVs), whose dynamics are controlled by Ca²⁺-dependent pathways, as many thoroughly studied phosphorylation cascades. However, little is known about other post-translational modifications, such as ubiquitination. To address this, we analyzed resting and stimulated synaptosomes (isolated synapses) by quantitative mass spectrometry. We identified more than 5000 ubiquitination sites on ∼2000 proteins, the majority of which participate in SV recycling processes. Several proteins showed significant changes in ubiquitination in response to Ca²⁺ influx, with the most pronounced changes in CaMKIIα and the clathrin adaptor protein AP180. To validate this finding, we generated a CaMKIIα mutant lacking the ubiquitination target site (K291) and analyzed it both in neurons and non-neuronal cells. K291 ubiquitination, close to an important site for CaMKIIα autophosphorylation (T286), influences the synaptic function of this kinase. We suggest that ubiquitination in response to synaptic activity is an important regulator of synaptic function.

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SNAP91

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