Annexins are Ca++ dependant phospholipids-binding proteins. Annexins form a multi-membered superfamily whose constituents are generally cytosolic, and are implicated in functions such as membrane organization, exocytosis, endocytosis, ion fluxes, signal transduction etc.
Moss and Morgan, Genome Biology 5:219
Gerke and Moss, Physiol Rev 82: 331-371
Annexin A1 (Annexin 1 or Lipocortin) has been implicated in the regulation of phagocytosis, cell signaling, proliferation, inflammation and control of anterior pituitary hormone release. A requirement for Annexin A1 in Ca++ induced plasma membrane repair has also been described.
McNeil et al., JBC 281 (46): 35202-35207
Annexin A2 (Annexin II or Calpactin) plays a role in functions such as vesicle trafficking, osteoclast formation and bone resorption, and anticoagulant reactions.
Annexin A6 binds to skeletal muscle at the triad junctions, goes to the sarcolemma following injury in zebra fish and increases opening time of ryanodine receptors in smooth muscle (this is not known for skeletal muscle). Annexin A6 morphant zebrafish exhibit a muscle pathology similar to dysferlin deficiency.