Structural highlights
Function
[LSP1_YEAST] Together with PIL1, main component of eisosomes, structures at the cell periphery underneath the plasma membrane that mark the site of endocytosis. Negative regulator of cell wall integrity (CWI) in unstressed cells, probably by inhibiting protein kinase PKH1/PHK2 activity and regulating their downstream CWI pathways PKC1-MAP kinase pathway and protein kinase YPK1 pathway. Activity may be regulated by the transient increase of sphingolipid long chain bases (LCBs) during heat stress.[1]
Publication Abstract from PubMed
Plasma membranes are organized into domains of different protein and lipid composition. Eisosomes are key complexes for yeast plasma membrane organization, containing primarily Pil1 and Lsp1. Here we show that both proteins consist mostly of a banana-shaped BAR domain common to membrane sculpting proteins, most similar to the ones of amphiphysin, arfaptin 2 and endophilin 2. Our data reveal a previously unrecognized family of BAR-domain proteins involved in plasma membrane organization.
Eisosome-driven plasma membrane organization is mediated by BAR domains.,Ziolkowska NE, Karotki L, Rehman M, Huiskonen JT, Walther TC Nat Struct Mol Biol. 2011 Jun 19. doi: 10.1038/nsmb.2080. PMID:21685922[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Zhang X, Lester RL, Dickson RC. Pil1p and Lsp1p negatively regulate the 3-phosphoinositide-dependent protein kinase-like kinase Pkh1p and downstream signaling pathways Pkc1p and Ypk1p. J Biol Chem. 2004 May 21;279(21):22030-8. Epub 2004 Mar 11. PMID:15016821 doi:http://dx.doi.org/10.1074/jbc.M400299200
- ↑ Ziolkowska NE, Karotki L, Rehman M, Huiskonen JT, Walther TC. Eisosome-driven plasma membrane organization is mediated by BAR domains. Nat Struct Mol Biol. 2011 Jun 19. doi: 10.1038/nsmb.2080. PMID:21685922 doi:10.1038/nsmb.2080
