Annexin: Difference between revisions
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[[Annexin|Annexins]] are proteins which make a membrane scaffold. They bind negatively charged phospholipids and contain a 70 amino acid long annexin repeat. Annexins divide into species and are numbered from I to XII. | [[Annexin|Annexins]] are proteins which make a membrane scaffold. They bind negatively charged phospholipids and contain a 70 amino acid long annexin repeat. Annexins divide into species and are numbered from I to XII. | ||
*'''Annexin I''' is involved in a variety of pathways<ref>PMID:17215481</ref>. <br /> | *'''Annexin I''' is involved in a variety of pathways<ref>PMID:17215481</ref>. <br /> | ||
*'''Annexin II''' is involved in angiogenesis, tutor progression and metastasis<ref>PMID:18220793</ref>. <br /> | *'''Annexin II''' is involved in angiogenesis, tutor progression and metastasis<ref>PMID:18220793</ref>. See also [[Ezetimibe]].<br /><br /> | ||
*'''Annexin V''' is the most abundant scaffolding protein. <br /> | *'''Annexin V''' is the most abundant scaffolding protein. <br /> | ||
*'''Annexin VI''' is involved in endocytosis and regulates entry of ligands to prelysosomal compartment<ref>PMID:10940299</ref>. <br /> | |||
*'''Annexin E1''' (AnE1) is associated with tubulin in trophozoites of ''Giardia lamblia'' and forms local slubs in the flagella. <br /> | *'''Annexin E1''' (AnE1) is associated with tubulin in trophozoites of ''Giardia lamblia'' and forms local slubs in the flagella. <br /> | ||
*'''Annexin A-V''' has a major role in coagulation. <br /> | *'''Annexin A-V''' has a major role in coagulation. <br /> | ||
== Relevance == | == Relevance == | ||
Revision as of 12:54, 26 May 2024
FunctionAnnexins are proteins which make a membrane scaffold. They bind negatively charged phospholipids and contain a 70 amino acid long annexin repeat. Annexins divide into species and are numbered from I to XII.
RelevanceAnnexin I is involved in anti-inflammatory responses and apoptotic mechanisms. Structural highlightsAnnexins consist of 2 domains - the C-terminal core and the N-terminal head. The containing . The core domain concave side contains the .[4] 3D structures of annexin
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ReferencesReferences
- ↑ Lim LH, Pervaiz S. Annexin 1: the new face of an old molecule. FASEB J. 2007 Apr;21(4):968-75. PMID:17215481 doi:10.1096/fj.06-7464rev
- ↑ Sharma MC, Sharma M. The role of annexin II in angiogenesis and tumor progression: a potential therapeutic target. Curr Pharm Des. 2007;13(35):3568-75. PMID:18220793 doi:10.2174/138161207782794167
- ↑ Grewal T, Heeren J, Mewawala D, Schnitgerhans T, Wendt D, Salomon G, Enrich C, Beisiegel U, Jäckle S. Annexin VI stimulates endocytosis and is involved in the trafficking of low density lipoprotein to the prelysosomal compartment. J Biol Chem. 2000 Oct 27;275(43):33806-13. PMID:10940299 doi:10.1074/jbc.M002662200
- ↑ Mo Y, Campos B, Mealy TR, Commodore L, Head JF, Dedman JR, Seaton BA. Interfacial basic cluster in annexin V couples phospholipid binding and trimer formation on membrane surfaces. J Biol Chem. 2003 Jan 24;278(4):2437-43. Epub 2002 Oct 24. PMID:12401794 doi:10.1074/jbc.M210286200