Annexin A6—Linking Ca2+ signaling with cholesterol transport
نویسندگان
چکیده
منابع مشابه
Apolipoprotein E: a cholesterol transport protein with lipid transport-independent cell signaling properties.
Apolipoprotein (apo) E is a 34-kDa glycoprotein associated with plasma lipoproteins. In contrast to other apolipoproteins, apoE is expressed ubiquitously in all tissues and appears to have a wide variety of functions in addition to lipid transport. Although the lipid transport properties of apoE are well characterized, the appreciation apoE functions other than lipid transport is still in an in...
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Membrane contact sites between the ER and multivesicular endosomes/bodies (MVBs) play important roles in endosome positioning and fission and in neurite outgrowth. ER-MVB contacts additionally function in epidermal growth factor receptor (EGFR) tyrosine kinase downregulation by providing sites where the ER-localized phosphatase, PTP1B, interacts with endocytosed EGFR before the receptor is sort...
متن کاملAnnexin A6-Induced Alterations in Cholesterol Transport and Caveolin Export from the Golgi Complex
Annexin A6 (AnxA6) belongs to a family of Ca(2+)-dependent membrane-binding proteins and is involved in the regulation of endocytic and exocytic pathways. We previously demonstrated that AnxA6 regulates receptor-mediated endocytosis and lysosomal targeting of low-density lipoproteins and translocates to cholesterol-enriched late endosomes (LE). As cholesterol modulates the membrane binding and ...
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The molecular details of how cholesterol exits lysosomes and is integrated into cellular and endoplasmic reticulum membranes remain unclear. Two proteins implicated in this exit process, the 13-transmembrane transporter NPC1 and secreted NPC2, are known to be mutated in Niemann-Pick type C (NPC) disease in humans, characterized by cholesterol accumulation. A recent X-ray crystallographic study ...
متن کاملCa2+-dependent and phospholipid-independent binding of annexin 2 and annexin 5.
Annexins are a family of homologous proteins that associate with anionic phospholipid (aPL) in the presence of Ca(2+). Evidence that the function of one annexin type may be regulated by another was recently reported in studies investigating cytomegalovirus-aPL interactions, where the fusogenic function of annexin 2 (A2) was attenuated by annexin 5 (A5). This observation suggested that A2 may bi...
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ژورنال
عنوان ژورنال: Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
سال: 2011
ISSN: 0167-4889
DOI: 10.1016/j.bbamcr.2010.09.015