Short transient receptor potential channel: Difference between revisions
From Proteopedia
Jump to navigationJump to search
Michal Harel (talk | contribs) No edit summary |
Michal Harel (talk | contribs) No edit summary |
||
| Line 9: | Line 9: | ||
1.'''TRPC1''' helps the cell to fill up for SERCA2 deficiency so that the cell can survive by letting more calcium enter the endoplasmic reticulum. This activates survival pathways, such as NF-kB, reduces cell death, and promotes cell growth.<ref>Pani, B., Cornatzer, E. et al. (2006). Up-Regulation of Transient Receptor Potential Canonical 1 (TRPC1) following Sarco(endo)plasmic Reticulum Ca²⁺ ATPase 2 Gene Silencing Promotes Cell Survival: A Potential Role for TRPC1 in Darier's Disease. ''Molecular Biology of the Cell'', 17(10):4446–4458.</ref> | 1.'''TRPC1''' helps the cell to fill up for SERCA2 deficiency so that the cell can survive by letting more calcium enter the endoplasmic reticulum. This activates survival pathways, such as NF-kB, reduces cell death, and promotes cell growth.<ref>Pani, B., Cornatzer, E. et al. (2006). Up-Regulation of Transient Receptor Potential Canonical 1 (TRPC1) following Sarco(endo)plasmic Reticulum Ca²⁺ ATPase 2 Gene Silencing Promotes Cell Survival: A Potential Role for TRPC1 in Darier's Disease. ''Molecular Biology of the Cell'', 17(10):4446–4458.</ref> | ||
2) when TRPC1 joins TRPC4 channel (1 TRPC1 and TRPC4) it pushes away Ca²⁺ as TRPC1 has an aminio acid(K639) which is positively charged pushing the positively charged calcium. It also develops more preference for Na⁺/K⁺ over Ca²⁺, while increasing inhibitor sensitivity.<ref>Won, J., Kim, J., Kim, J. et al. (2025). Cryo-EM structure of the heteromeric TRPC1/TRPC4 channel. ''Nature Structural & Molecular Biology'', 32(2):326–338. DOI: 10.1038/s41594-024-01408-1</ref> | 2) when TRPC1 joins TRPC4 channel (1 TRPC1 and TRPC4) it pushes away Ca²⁺ as TRPC1 has an aminio acid(K639) which is positively charged pushing the positively charged calcium. It also develops more preference for Na⁺/K⁺ over Ca²⁺, while increasing inhibitor sensitivity.<ref>Won, J., Kim, J., Kim, J. et al. (2025). Cryo-EM structure of the heteromeric TRPC1/TRPC4 channel. ''Nature Structural & Molecular Biology'', 32(2):326–338. DOI: 10.1038/s41594-024-01408-1</ref> | ||
3. '''TRPC4''' is essential during early postnatal brain development, as it helps dendrites grow and stay stable by turning glutamate signals into calcium entry, activating a force-generating pathway. Without TRPC4, dendrites will disintegrate.<ref>Jeon, J., Moore, T. I., Sob, I. et al. (2025). TRPC4 regulates limbic behavior and neuronal development by stabilizing dendrite branches through actomyosin-driven integrin activation. ''PNAS'', 122(33):e2511037ca122.</ref> | 3. '''TRPC4''' is essential during early postnatal brain development, as it helps dendrites grow and stay stable by turning glutamate signals into calcium entry, activating a force-generating pathway. Without TRPC4, dendrites will disintegrate.<ref>Jeon, J., Moore, T. I., Sob, I. et al. (2025). TRPC4 regulates limbic behavior and neuronal development by stabilizing dendrite branches through actomyosin-driven integrin activation. ''PNAS'', 122(33):e2511037ca122.</ref> | ||
