Abstract:
:We have previously shown that plasma membrane calcium ATPase (PMCA) pump activity is affected by the membrane protein concentration (Vanagas et al., Biochim Biophys Acta 1768:1641-1644, 2007). The results of this study provided evidence for the involvement of the actin cytoskeleton. In this study, we explored the relationship between the polymerization state of actin and its effects on purified PMCA activity. Our results show that PMCA associates with the actin cytoskeleton and this interaction causes a modulation of the catalytic activity involving the phosphorylated intermediate of the pump. The state of actin polymerization determines whether it acts as an activator or an inhibitor of the pump: G-actin and/or short oligomers activate the pump, while F-actin inhibits it. The effects of actin on PMCA are the consequence of direct interaction as demonstrated by immunoblotting and cosedimentation experiments. Taken together, these findings suggest that interactions with actin play a dynamic role in the regulation of PMCA-mediated Ca(2+) extrusion through the membrane. Our results provide further evidence of the activation-inhibition phenomenon as a property of many cytoskeleton-associated membrane proteins where the cytoskeleton is no longer restricted to a mechanical function but is dynamically involved in modulating the activity of integral proteins with which it interacts.
journal_name
Cell Biochem Biophysjournal_title
Cell biochemistry and biophysicsauthors
Vanagas L,de La Fuente MC,Dalghi M,Ferreira-Gomes M,Rossi RC,Strehler EE,Mangialavori IC,Rossi JPdoi
10.1007/s12013-012-9467-6subject
Has Abstractpub_date
2013-05-01 00:00:00pages
187-98issue
1eissn
1085-9195issn
1559-0283journal_volume
66pub_type
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