@article {47574,
	title = {Caveolin induced membrane curvature and lipid clustering: two sides of the same coin?},
	journal = {Faraday Discussions},
	volume = {232},
	year = {2021},
	month = {DEC},
	pages = {218-235},
	type = {Article},
	abstract = {Caveolin-1 (cav-1) is a multi-domain membrane protein that is a key player in cell signaling, endocytosis and mechanoprotection. It is the principle component of cholesterol-rich caveolar domains and has been reported to induce membrane curvature. The molecular mechanisms underlying the interactions of cav-1 with complex membranes, leading to modulation of membrane topology and the formation of cholesterol-rich domains, remain elusive. In this study, we aim to understand the effect of lipid composition by analyzing the interactions of cav-1 with complex membrane bilayers comprised of about sixty lipid types. We have performed a series of coarse-grain molecular dynamics simulations using the Martini force-field with a cav-1 protein construct (residue 82-136) that includes the membrane binding domains and a palmitoyl tail. We observe that cav-1 induces curvature in this complex membrane, though it is restricted to a nanometer length scale. Concurrently, we observe a clustering of cholesterol, sphingolipids and other lipid molecules leading to the formation of nanodomains. Direct microsecond timescale interactions are observed for specific lipids such as cholesterol, phosphatidylserine and phosphatidylethanolamine lipid types. The results indicate that there is an interplay between membrane topology and lipid species. Our work is a step toward understanding how lipid composition and organization regulate the formation of caveolae, in the context of endocytosis and cell signaling.},
	issn = {1359-6640},
	doi = {10.1039/d0fd00062k},
	author = {Prakash, Shikha and Krishna, Anjali and Sengupta, Durba}
}
@article {47431,
	title = {Caveolin mediated curvature and clustering: from simple to complex membrane},
	journal = {Biophysical Journal},
	volume = {120},
	year = {2021},
	month = {FEB },
	pages = {232A-233A},
	type = {Meeting Abstract},
	issn = {0006-3495},
	doi = {10.1016/j.bpj.2020.11.1542},
	author = {Prakash, Shikha and Krishna, Anjali and Sengupta, Durba}
}
@article {48442,
	title = {Cofilin-membrane interactions: electrostatic effects in phosphoinositide lipid binding},
	journal = {ChemPhysChem},
	volume = {24},
	year = {2023},
	month = {FEB },
	type = {Article},
	abstract = {<p>
	The actin cytoskeleton interacts with the cell membrane primarily through the indirect interactions of actin-binding proteins such as cofilin-1. The molecular mechanisms underlying the specific interactions of cofilin-1 with membrane lipids are still unclear. Here, we performed coarse-grain molecular dynamics simulations of cofilin-1 with complex lipid bilayers to analyze the specificity of protein-lipid interactions. We observed the maximal interactions with phosphoinositide (PIP) lipids, especially PIP2 and PIP3 lipids. A good match was observed between the residues predicted to interact and previous experimental studies. The clustering of PIP lipids around the membrane bound protein leads to an overall lipid demixing and gives rise to persistent membrane curvature. Further, through a series of control simulations, we observe that both electrostatics and geometry are critical for specificity of lipid binding. Our current study is a step towards understanding the physico-chemical basis of cofilin-PIP lipid interactions.</p>
},
	keywords = {complex membrane, lipid clustering, Martini coarse-grain simulations, Molecular dynamics simulations, Protein-lipid interactions},
	issn = {1439-4235},
	doi = {10.1002/cphc.202200509},
	author = {Prakash, Shikha and Krishna, Anjali and Sengupta, Durba}
}
