Abstract:
:Annexins, found in most eukaryotic species, are cytosolic proteins that are able to bind negatively-charged phospholipids in a calcium-dependent manner. Annexin A4 (AnxA4) has been implicated in diverse cellular processes, including the regulation of exocytosis and ion-transport; however, its precise mechanistic role is not fully understood. AnxA4 has been shown to aggregate on lipid layers upon Ca(2+) binding in vitro, a characteristic that may be critical for its function. We have utilized advanced fluorescence microscopy to discern details on the mobility and self-assembly of AnxA4 after Ca(2+) influx at the plasma membrane in living cells. Total internal reflection microscopy in combination with Förster resonance energy transfer reveals that there is a delay between initial plasma membrane binding and the beginning of self-assembly and this process continues after the cytoplasmic pool has completely relocated. Number-and-brightness analysis suggests that the predominant membrane bound mobile form of the protein is trimeric. There also exists a pool of AnxA4 that forms highly immobile aggregates at the membrane. Fluorescence recovery after photobleaching suggests that the relative proportion of these two forms varies and is correlated with membrane morphology.
journal_name
Biophys Jjournal_title
Biophysical journalauthors
Crosby KC,Postma M,Hink MA,Zeelenberg CH,Adjobo-Hermans MJ,Gadella TWdoi
10.1016/j.bpj.2013.02.057subject
Has Abstractpub_date
2013-05-07 00:00:00pages
1875-85issue
9eissn
0006-3495issn
1542-0086pii
S0006-3495(13)00365-2journal_volume
104pub_type
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