CLSTN1
Appearance
Template:PBB Calsyntenin-1 is a protein that in humans is encoded by the CLSTN1 gene.[1][2]
Clinical relevance
Mutations in this gene have been shown associated to pathogenic mechanisms of Alzheimer's disease.[3]
Interactions
CLSTN1 has been shown to interact with APBA2[4][5] and Amyloid precursor protein.[4][5]
References
- ^ Nagase T, Ishikawa K, Suyama M, Kikuno R, Hirosawa M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O (Dec 1998). "Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro". DNA Research. 5 (6): 355–64. doi:10.1093/dnares/5.6.355. PMID 10048485.
- ^ "Entrez Gene: CLSTN1 calsyntenin 1".
- ^ Vagnoni A, Perkinton MS, Gray EH, Francis PT, Noble W, Miller CC (Jul 2012). "Calsyntenin-1 mediates axonal transport of the amyloid precursor protein and regulates Aβ production". Human Molecular Genetics. 21 (13): 2845–54. doi:10.1093/hmg/dds109. PMID 22434822.
- ^ a b Araki Y, Tomita S, Yamaguchi H, Miyagi N, Sumioka A, Kirino Y, Suzuki T (Dec 2003). "Novel cadherin-related membrane proteins, Alcadeins, enhance the X11-like protein-mediated stabilization of amyloid beta-protein precursor metabolism". The Journal of Biological Chemistry. 278 (49): 49448–58. doi:10.1074/jbc.M306024200. PMID 12972431.
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: CS1 maint: unflagged free DOI (link) - ^ a b Araki Y, Miyagi N, Kato N, Yoshida T, Wada S, Nishimura M, Komano H, Yamamoto T, De Strooper B, Yamamoto K, Suzuki T (Jun 2004). "Coordinated metabolism of Alcadein and amyloid beta-protein precursor regulates FE65-dependent gene transactivation". The Journal of Biological Chemistry. 279 (23): 24343–54. doi:10.1074/jbc.M401925200. PMID 15037614.
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: CS1 maint: unflagged free DOI (link)
Further reading
- Konecna A, Frischknecht R, Kinter J, Ludwig A, Steuble M, Meskenaite V, Indermühle M, Engel M, Cen C, Mateos JM, Streit P, Sonderegger P (Aug 2006). "Calsyntenin-1 docks vesicular cargo to kinesin-1". Molecular Biology of the Cell. 17 (8): 3651–63. doi:10.1091/mbc.E06-02-0112. PMC 1525238. PMID 16760430.
- Schmitt-Ulms G, Hansen K, Liu J, Cowdrey C, Yang J, DeArmond SJ, Cohen FE, Prusiner SB, Baldwin MA (Jun 2004). "Time-controlled transcardiac perfusion cross-linking for the study of protein interactions in complex tissues". Nature Biotechnology. 22 (6): 724–31. doi:10.1038/nbt969. PMID 15146195.
- Araki Y, Miyagi N, Kato N, Yoshida T, Wada S, Nishimura M, Komano H, Yamamoto T, De Strooper B, Yamamoto K, Suzuki T (Jun 2004). "Coordinated metabolism of Alcadein and amyloid beta-protein precursor regulates FE65-dependent gene transactivation". The Journal of Biological Chemistry. 279 (23): 24343–54. doi:10.1074/jbc.M401925200. PMID 15037614.
{{cite journal}}
: CS1 maint: unflagged free DOI (link) - Araki Y, Tomita S, Yamaguchi H, Miyagi N, Sumioka A, Kirino Y, Suzuki T (Dec 2003). "Novel cadherin-related membrane proteins, Alcadeins, enhance the X11-like protein-mediated stabilization of amyloid beta-protein precursor metabolism". The Journal of Biological Chemistry. 278 (49): 49448–58. doi:10.1074/jbc.M306024200. PMID 12972431.
{{cite journal}}
: CS1 maint: unflagged free DOI (link) - Nakayama M, Kikuno R, Ohara O (Nov 2002). "Protein-protein interactions between large proteins: two-hybrid screening using a functionally classified library composed of long cDNAs". Genome Research. 12 (11): 1773–84. doi:10.1101/gr.406902. PMC 187542. PMID 12421765.
- Vogt L, Schrimpf SP, Meskenaite V, Frischknecht R, Kinter J, Leone DP, Ziegler U, Sonderegger P (Jan 2001). "Calsyntenin-1, a proteolytically processed postsynaptic membrane protein with a cytoplasmic calcium-binding domain". Molecular and Cellular Neurosciences. 17 (1): 151–66. doi:10.1006/mcne.2000.0937. PMID 11161476.
- Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (Oct 1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
- Maruyama K, Sugano S (Jan 1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.