Annexin A8 displays unique phospholipid and F-actin binding properties
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چکیده
منابع مشابه
Staphylococcal enterotoxin H displays unique MHC class II-binding properties.
Staphylococcal enterotoxin H (SEH) has been described as a superantigen by sequence homology with the SEA subfamily and briefly characterized for its in vivo activity. In this study, we demonstrate that SEH is a potent T cell mitogen and inducer of T cell cytotoxicity that possesses unique MHC class II-binding properties. The apparent affinity of SEH for MHC class II molecules is the highest af...
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...
متن کاملAnnexin V, a calcium-dependent phospholipid-binding protein.
828 Introduction Calcium regulates cellular processes by interacting with calcium-binding proteins. Two major families of calcium-binding proteins have been identified: The E-F hand proteins, which include calmodulin, SlOO and calcyclin; and the annexins (see [ l ] for review, and [2] for annexin nomenclature). Both families constitute major pools of calcium-binding activity. They are found in ...
متن کاملClass-specific binding of two aminoacyl-tRNA synthetases to annexin, a Ca2+- and phospholipid-binding protein.
Annexins are a family of Ca2+/phospholipid-binding proteins that have diverse functions. To understand the function of annexin in Physarum polycephalum, we searched for its binding proteins. Here we demonstrate the presence of two novel annexin-binding proteins. The homology search of partial amino acid sequences of these two proteins identified them as aminoacyl-tRNA synthetases (ARSs). Furthe...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 2006
ISSN: 0014-5793
DOI: 10.1016/j.febslet.2006.03.076