| SNAPIN Regulates Cell Cycle Progression to Promote Pancreatic beta Cell Growth. | SNAPIN Regulates Cell Cycle Progression to Promote Pancreatic β Cell Growth.
Jiang M, Kuang Z, He Y, Cao Y, Yu T, Cheng J, Liu W, Wang W., Free PMC Article | 12/18/2021 |
| Snapin Specifically Up-Regulates Cav1.3 Ca(2+) Channel Variant with a Long Carboxyl Terminus. | Snapin Specifically Up-Regulates Ca(v)1.3 Ca(2+) Channel Variant with a Long Carboxyl Terminus.
Jeong S, Rhee JS, Lee JH., Free PMC Article | 12/18/2021 |
| These observations suggest an important role for SNAPIN and autophagy in the homeostasis of macrophages, particularly long-lived tissue resident macrophages. | SNAPIN is critical for lysosomal acidification and autophagosome maturation in macrophages.
Shi B, Huang QQ, Birkett R, Doyle R, Dorfleutner A, Stehlik C, He C, Pope RM., Free PMC Article | 12/2/2017 |
| These results provide the evidence of a direct regulatory role of Snapin on Cav1.3 channels in atrial myocytes. | Physical and functional interaction of Snapin with Cav1.3 calcium channel impacts channel protein trafficking in atrial myocytes.
Sun XL, Yuan JF, Jin T, Cheng XQ, Wang Q, Guo J, Zhang W, Zhang Y, Lu L, Zhang Z. | 12/2/2017 |
| Inhibition of Snapin enhanced localization of HIV-1 with TLR8(+) early endosomes, triggered a pro-inflammatory response, and inhibited trans-infection of CD4(+) T cells. | Snapin promotes HIV-1 transmission from dendritic cells by dampening TLR8 signaling.
Khatamzas E, Hipp MM, Gaughan D, Pichulik T, Leslie A, Fernandes RA, Muraro D, Booth S, Zausmer K, Sun MY, Kessler B, Rowland-Jones S, Cerundolo V, Simmons A., Free PMC Article | 10/21/2017 |
| Taken together, these results suggest that Snapin, the pUL130 interacting protein, has a role in modulating HCMV DNA synthesis. | Host protein Snapin interacts with human cytomegalovirus pUL130 and affects viral DNA replication.
Wang G, Ren G, Cui X, Lu Z, Ma Y, Qi Y, Huang Y, Liu Z, Sun Z, Ruan Q. | 03/25/2017 |
| Disruption of Snapin-PKR2 interaction did not affect PKR2 signaling, but increased the ligand-induced degradation, implying a role of Snapin in the trafficking of PKR2. | Snapin interacts with G-protein coupled receptor PKR2.
Song J, Li J, Liu HD, Liu W, Feng Y, Zhou XT, Li JD. | 05/28/2016 |
| Authors propose that Snapin connects chlamydial inclusions with the microtubule network by interacting with both Chlamydia psittaci IncB and dynein. | Chlamydia psittaci inclusion membrane protein IncB associates with host protein Snapin.
Böcker S, Heurich A, Franke C, Monajembashi S, Sachse K, Saluz HP, Hänel F. | 02/21/2015 |
| Snapin, a SNAP-25 (synaptosomal-associated protein-25) interacting protein, interacts with LRRK2. | LRRK2 phosphorylates Snapin and inhibits interaction of Snapin with SNAP-25.
Yun HJ, Park J, Ho DH, Kim H, Kim CH, Oh H, Ga I, Seo H, Chang S, Son I, Seol W., Free PMC Article | 10/26/2013 |
| Our findings reveal that Atg14L, previously considered to be solely a Beclin 1-binding autophagy protein, plays a novel role in the late stage of endocytic trafficking in conjunction with Snapin | Beclin-1-interacting autophagy protein Atg14L targets the SNARE-associated protein Snapin to coordinate endocytic trafficking.
Kim HJ, Zhong Q, Sheng ZH, Yoshimori T, Liang C, Jung JU., Free PMC Article | 06/1/2013 |
| These observations identify Snapin as a novel endogenous TLR2 ligand in rheumatoid arthritis, and thus support a role for persistent TLR2 signalling in pathogenesis. | SNAPIN: an endogenous Toll-like receptor ligand in rheumatoid arthritis.
Shi B, Huang Q, Tak PP, Vervoordeldonk MJ, Huang CC, Dorfleutner A, Stehlik C, Pope RM. | 09/29/2012 |
| These results suggest that Snapin may play a key role in regulating the cellular localization of human cytomegalovirus UL70, leading to modulation of viral DNA synthesis and progeny production. | Human cytomegalovirus primase UL70 specifically interacts with cellular factor Snapin.
Shen A, Lei J, Yang E, Pei Y, Chen YC, Gong H, Xiao G, Liu F., Free PMC Article | 12/17/2011 |
| PKA-dependent phosphorylation of snapin increases interaction among insulin secretory vesicle-associated proteins, thereby potentiating glucose-stimulated insulin secretion. | Snapin mediates incretin action and augments glucose-dependent insulin secretion.
Song WJ, Seshadri M, Ashraf U, Mdluli T, Mondal P, Keil M, Azevedo M, Kirschner LS, Stratakis CA, Hussain MA., Free PMC Article | 06/18/2011 |
| Observational study of gene-disease association. (HuGE Navigator) | New genetic associations detected in a host response study to hepatitis B vaccine.
Davila S, Froeling FE, Tan A, Bonnard C, Boland GJ, Snippe H, Hibberd ML, Seielstad M. | 04/7/2010 |
| Snapin plays an important role as a linker between the water channel and the t-SNARE complex, leading to the fusion event, and the pairing with specific t-SNAREs is essential for the specificity of membrane recognition and fusion. | Syntaxin specificity of aquaporins in the inner medullary collecting duct.
Mistry AC, Mallick R, Klein JD, Weimbs T, Sands JM, Fröhlich O., Free PMC Article | 01/21/2010 |
| Data describe for the first time the expression of SNAPIN in germ cells which raises possibility that SNAPIN plays an extra role in mammals which is germ cell specific. | The SNARE-associated component SNAPIN binds PUMILIO2 and NANOS1 proteins in human male germ cells.
Ginter-Matuszewska B, Spik A, Rembiszewska A, Koyias C, Kupryjanczyk J, Jaruzelska J. | 01/21/2010 |
| Snapin links the alpha(1A)-AR to TRPC6, augmenting Ca(2+) influx via ROC channels | Snapin, a new regulator of receptor signaling, augments alpha1A-adrenoceptor-operated calcium influx through TRPC6.
Suzuki F, Morishima S, Tanaka T, Muramatsu I. | 01/21/2010 |
| results demonstrate that snapin is a binding partner of dysbindin-1 in vitro and in the brain; both dysbindin-1 and snapin are concentrated in tissue enriched in synaptic vesicle membranes and less commonly in postsynaptic densities | Dysbindin-1 is a synaptic and microtubular protein that binds brain snapin.
Talbot K, Cho DS, Ong WY, Benson MA, Han LY, Kazi HA, Kamins J, Hahn CG, Blake DJ, Arnold SE. | 01/21/2010 |
| results suggest that RGS7 could play a role in synaptic vesicle exocytosis through its interaction with snapin | Snapin interacts with the N-terminus of regulator of G protein signaling 7.
Hunt RA, Edris W, Chanda PK, Nieuwenhuijsen B, Young KH. | 01/21/2010 |
| EBAG9 and Snapin have roles in controlling exocytosis processes | EBAG9 adds a new layer of control on large dense-core vesicle exocytosis via interaction with Snapin.
Rüder C, Reimer T, Delgado-Martinez I, Hermosilla R, Engelsberg A, Nehring R, Dörken B, Rehm A., Free PMC Article | 01/21/2010 |