SLA2/YNL243W Literature Guide Help

Other names published for SLA2: END4, MOP2, YNL243W

SLA2 - Protein Sequence Features (23)

ReferenceOther Genes Addressed
Skruzny M, et al.  (2012) Molecular basis for coupling the plasma membrane to the actin cytoskeleton during clathrin-mediated endocytosis. Proc Natl Acad Sci U S A 109(38):E2533-42
Boettner DR, et al.  (2011) Clathrin light chain directs endocytosis by influencing the binding of the yeast Hip1R homologue, Sla2, to F-actin. Mol Biol Cell 22(19):3699-714
Gallego O, et al.  (2010) A systematic screen for protein-lipid interactions in Saccharomyces cerevisiae. Mol Syst Biol 6():430
Mathur V, et al.  (2010) Analyzing the birth and propagation of two distinct prions, [PSI+] and [Het-s](y), in yeast. Mol Biol Cell 21(9):1449-61
Yamamoto T, et al.  (2010) Initial polarized bud growth by endocytic recycling in the absence of actin cable-dependent vesicle transport in yeast. Mol Biol Cell 21(7):1237-52
Smaczynska-de Rooij II, et al.  (2008) Yeast Arf3p Modulates Plasma Membrane PtdIns(4,5)P2 Levels to Facilitate Endocytosis. Traffic 9(4):559-73
Toshima J, et al.  (2007) Negative regulation of yeast Eps15-like Arp2/3 complex activator, Pan1p, by the Hip1R-related protein, Sla2p, during endocytosis. Mol Biol Cell 18(2):658-68
Ganusova EE, et al.  (2006) Modulation of prion formation, aggregation, and toxicity by the actin cytoskeleton in yeast. Mol Cell Biol 26(2):617-29
Newpher TM and Lemmon SK  (2006) Clathrin is important for normal actin dynamics and progression of Sla2p-containing patches during endocytosis in yeast. Traffic 7(5):574-88
Newpher TM, et al.  (2006) Novel function of clathrin light chain in promoting endocytic vesicle formation. Mol Biol Cell 17(10):4343-52
Pitre S, et al.  (2006) PIPE: a protein-protein interaction prediction engine based on the re-occurring short polypeptide sequences between known interacting protein pairs. BMC Bioinformatics 7():365
Yoshiuchi S, et al.  (2006) Identification of novel mutations in ACT1 and SLA2 that suppress the actin-cable-overproducing phenotype caused by overexpression of a dominant active form of Bni1p in Saccharomyces cerevisiae. Genetics 173(2):527-39
Sun Y, et al.  (2005) Interaction of Sla2p's ANTH domain with PtdIns(4,5)P2 is important for actin-dependent endocytic internalization. Mol Biol Cell 16(2):717-30
Chidambaram S, et al.  (2004) Specific interaction between SNAREs and epsin N-terminal homology (ENTH) domains of epsin-related proteins in trans-Golgi network to endosome transport. J Biol Chem 279(6):4175-9
Baggett JJ, et al.  (2003) The Sla2p talin domain plays a role in endocytosis in Saccharomyces cerevisiae. Genetics 165(4):1661-74
Gourlay CW, et al.  (2003) An interaction between Sla1p and Sla2p plays a role in regulating actin dynamics and endocytosis in budding yeast. J Cell Sci 116(Pt 12):2551-64
Palecek J, et al.  (2001) Rpg1p/Tif32p, a subunit of translation initiation factor 3, interacts with actin-associated protein Sla2p. Biochem Biophys Res Commun 282(5):1244-50
McCann RO and Craig SW  (1999) Functional genomic analysis reveals the utility of the I/LWEQ module as a predictor of protein:actin interaction. Biochem Biophys Res Commun 266(1):135-40
Melms AS, et al.  (1999) Sequence analysis of SLA2 of the dimorphic yeasts Candida albicans and Yarrowia lipolytica. Yeast 15(14):1519-28
Yang S, et al.  (1999) Sla2p is associated with the yeast cortical actin cytoskeleton via redundant localization signals. Mol Biol Cell 10(7):2265-83
McCann RO and Craig SW  (1997) The I/LWEQ module: a conserved sequence that signifies F-actin binding in functionally diverse proteins from yeast to mammals. Proc Natl Acad Sci U S A 94(11):5679-84
Wesp A, et al.  (1997) End4p/Sla2p interacts with actin-associated proteins for endocytosis in Saccharomyces cerevisiae. Mol Biol Cell 8(11):2291-306
Holtzman DA, et al.  (1993) Synthetic-lethal interactions identify two novel genes, SLA1 and SLA2, that control membrane cytoskeleton assembly in Saccharomyces cerevisiae. J Cell Biol 122(3):635-44