Jump to content

Calsyntenin

From Wikipedia, the free encyclopedia

This is an old revision of this page, as edited by Tom.Reding (talk | contribs) at 16:28, 24 May 2016 (→‎top: CS1 maintenance: vauthors/veditors or enumerate multiple authors/editors using AWB). The present address (URL) is a permanent link to this revision, which may differ significantly from the current revision.

Calsyntenins (Csts, CLSTN) also known as alcadeins[1] are type I transmembrane proteins that belong to the cadherin superfamily. Their name comes from their ability to bind calcium. In birds and mammals, they consist of three family members (Cst1, 2 and 3),[2][3] in nematodes one ortholog (CASY-1, originally CDH11) is known.[4]

Cst1 (CLSTN1) was first shown to be predominantly expressed in postsynaptic membranes of excitatory neurons,[2] Cst2 and 3 were found in an increased manner in inhibitory GABAergic neurons.[3] Calsyntenins interact with numerous proteins such as with kinesin-1 and the APP-linker protein X11L/Mint2,[1][5][6] and were shown to have multi-purpose functions both within and outside the nervous system.[1][4][5][6][7]

Shortly after the calsyntenins were discovered, they were found to regulate postsynaptic calcium concentration.[2] Later it was found that another key-function is to link vesicles to kinesin light chain (KLC) and thus to co-determine transport of distinct cargo.[5][8]

References

  1. ^ a b c Araki Y, Tomita S, Yamaguchi H, Miyagi N, Sumioka A, Kirino Y, Suzuki T (December 2003). "Novel cadherin-related membrane proteins, Alcadeins, enhance the X11-like protein-mediated stabilization of amyloid beta-protein precursor metabolism". J. Biol. Chem. 278 (49): 49448–58. doi:10.1074/jbc.M306024200. PMID 12972431.{{cite journal}}: CS1 maint: unflagged free DOI (link)
  2. ^ a b c Vogt L, Schrimpf SP, Meskenaite V, Frischknecht R, Kinter J, Leone DP, Ziegler U, Sonderegger P (January 2001). "Calsyntenin-1, a proteolytically processed postsynaptic membrane protein with a cytoplasmic calcium-binding domain". Mol. Cell. Neurosci. 17 (1): 151–66. doi:10.1006/mcne.2000.0937. PMID 11161476.
  3. ^ a b Hintsch G, Zurlinden A, Meskenaite V, Steuble M, Fink-Widmer K, Kinter J, Sonderegger P (November 2002). "The calsyntenins--a family of postsynaptic membrane proteins with distinct neuronal expression patterns". Mol. Cell. Neurosci. 21 (3): 393–409. doi:10.1006/mcne.2002.1181. PMID 12498782.
  4. ^ a b Ikeda DD, Duan Y, Matsuki M, Kunitomo H, Hutter H, Hedgecock EM, Iino Y (April 2008). "CASY-1, an ortholog of calsyntenins/alcadeins, is essential for learning in Caenorhabditis elegans". Proc. Natl. Acad. Sci. U.S.A. 105 (13): 5260–5. doi:10.1073/pnas.0711894105. PMC 2278220. PMID 18381821.
  5. ^ a b c Konecna A, Frischknecht R, Kinter J, Ludwig A, Steuble M, Meskenaite V, Indermühle M, Engel M, Cen C, Mateos JM, Streit P, Sonderegger P (August 2006). "Calsyntenin-1 docks vesicular cargo to kinesin-1". Mol. Biol. Cell. 17 (8): 3651–63. doi:10.1091/mbc.E06-02-0112. PMC 1525238. PMID 16760430.
  6. ^ a b Rindler MJ, Xu CF, Gumper I, Cen C, Sonderegger P, Neubert TA (April 2008). "Calsyntenins are secretory granule proteins in anterior pituitary gland and pancreatic islet alpha cells". J. Histochem. Cytochem. 56 (4): 381–8. doi:10.1369/jhc.7A7351.2007. PMC 2326105. PMID 18158283.
  7. ^ Ludwig A, Blume J, Diep TM, Yuan J, Mateos JM, Leuthäuser K, Steuble M, Streit P, Sonderegger P (May 2009). "Calsyntenins mediate TGN exit of APP in a kinesin-1-dependent manner". Traffic. 10 (5): 572–89. doi:10.1111/j.1600-0854.2009.00886.x. PMID 19192245.
  8. ^ Steuble M, Gerrits B, Ludwig A, Mateos JM, Diep TM, Tagaya M, Stephan A, Schätzle P, Kunz B, Streit P, Sonderegger P (November 2010). "Molecular characterization of a trafficking organelle: dissecting the axonal paths of calsyntenin-1 transport vesicles". Proteomics. 10 (21): 3775–88. doi:10.1002/pmic.201000384. PMID 20925061.

External links