Anurima Majumder
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Research Subjects
Research Interests
Anurima Majumder has a total of 6 co-authors. Here are the top co-authors by number of shared publications:
- Alapakkam P. Sampath
Jules Stein Eye Institute David Geffen School of Medicine University of California Los Angeles California USA
1 shared publication - Gordon Fain
Department of Ophthalmology, Jules Stein Eye Institute, David Geffen School of Medicine, University of California Los Angeles, Los Angeles, USA
1 shared publication - Katherine E. Fehlhaber
Department of Ophthalmology, Jules Stein Eye Institute, University of California, Los Angeles, CA 90095, USA
1 shared publication - Khris G. Griffis
Department of Ophthalmology, Jules Stein Eye Institute, University of California, Los Angeles, CA 90095, USA
1 shared publication - Kimberly K. Boyd
Molecular Physiology and Biophysics, University of Iowa, Iowa City, IA 52242, USA
1 shared publication - Nikolai O. Artemyev
Department of Molecular Physiology and Biophysics, The University of Iowa Carver College of Medicine, Iowa City, IA 52242, USA; Department of Ophthalmology and Visual Sciences, The University of Iowa Carver College of Medicine, Iowa City, IA 52242, USA
1 shared publication
Latest Publications
- Open Access
- 30 April 2023
- Published by MDPI AG in International Journal of Molecular Sciences
- Vol. 24 (9) , 8106
A Novel Role for UNC119 as an Enhancer of Synaptic Transmission
Mammalian UNC119 is a ciliary trafficking chaperone highly expressed in the inner segment of retinal photoreceptors. Previous research has shown that UNC119 can bind to transducin, the synaptic ribbon protein RIBEYE, and the calcium-binding protein CaBP4, suggesting that UNC119 may have a role in synaptic transmission. We made patch-clamp recordings from retinal slices in mice with the UNC119 gene deleted and showed that removal of even one gene of UNC119 has no effect on the rod outer segment photocurrent, but acted on bipolar cells much like background light: it depolarized membrane potential, decreased sensitivity, accelerated response decay, and decreased the Hill coefficient of the response–intensity relationship. Similar effects were seen on rod bipolar-cell current and voltage responses, and after exposure to bright light to translocate transducin into the rod inner segment. These findings indicate that UNC119 deletion reduces the steady-state glutamate release rate at rod synapses, though no change in the voltage dependence of the synaptic Ca current was detected. We conclude that UNC119, either by itself or together with transducin, can facilitate the release of glutamate at rod synapses, probably by some interaction with RIBEYE or other synaptic proteins rather than by binding to CaBP4 or calcium channels.
- 30 April 2023
- Published by MDPI AG in International Journal of Molecular Sciences
- Vol. 24 (9) , 8106
Open AccessA Novel Role for UNC119 as an Enhancer of Synaptic Transmission
Mammalian UNC119 is a ciliary trafficking chaperone highly expressed in the inner segment of retinal photoreceptors. Previous research has shown that UNC119 can bind to transducin, the synaptic ribbon protein RIBEYE, and the calcium-binding protein CaBP4, suggesting that UNC119 may have a role in synaptic transmission. We made patch-clamp recordings from retinal slices in mice with the UNC119 gene deleted and showed that removal of even one gene of UNC119 has no effect on the rod outer segment photocurrent, but acted on bipolar cells much like background light: it depolarized membrane potential, decreased sensitivity, accelerated response decay, and decreased the Hill coefficient of the response–intensity relationship. Similar effects were seen on rod bipolar-cell current and voltage responses, and after exposure to bright light to translocate transducin into the rod inner segment. These findings indicate that UNC119 deletion reduces the steady-state glutamate release rate at rod synapses, though no change in the voltage dependence of the synaptic Ca current was detected. We conclude that UNC119, either by itself or together with transducin, can facilitate the release of glutamate at rod synapses, probably by some interaction with RIBEYE or other synaptic proteins rather than by binding to CaBP4 or calcium channels.