SLA2/YNL243W Literature Guide Help

Other names published for SLA2: END4, MOP2, YNL243W

SLA2 - Non-Fungal Related Genes/Proteins (13)

ReferenceOther Genes Addressed
Gallego O, et al.  (2010) A systematic screen for protein-lipid interactions in Saccharomyces cerevisiae. Mol Syst Biol 6():430
Niu Q and Ybe JA  (2008) Crystal structure at 2.8 A of Huntingtin-interacting protein 1 (HIP1) coiled-coil domain reveals a charged surface suitable for HIP1 protein interactor (HIPPI). J Mol Biol 375(5):1197-205
Ybe JA, et al.  (2007) Crystal structure at 2.8 A of the DLLRKN-containing coiled-coil domain of huntingtin-interacting protein 1 (HIP1) reveals a surface suitable for clathrin light chain binding. J Mol Biol 367(1):8-15
Tischler J, et al.  (2006) Combinatorial RNA interference in Caenorhabditis elegans reveals that redundancy between gene duplicates can be maintained for more than 80 million years of evolution. Genome Biol 7(8):R69
Henry KR, et al.  (2002) Scd5p and clathrin function are important for cortical actin organization, endocytosis, and localization of sla2p in yeast. Mol Biol Cell 13(8):2607-25
Chopra VS, et al.  (2000) HIP12 is a non-proapoptotic member of a gene family including HIP1, an interacting protein with huntingtin. Mamm Genome 11(11):1006-15
Hackam AS, et al.  (2000) Huntingtin interacting protein 1 induces apoptosis via a novel caspase-dependent death effector domain. J Biol Chem 275(52):41299-308
Engqvist-Goldstein AE, et al.  (1999) An actin-binding protein of the Sla2/Huntingtin interacting protein 1 family is a novel component of clathrin-coated pits and vesicles. J Cell Biol 147(7):1503-18
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
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
Kalchman MA, et al.  (1997) HIP1, a human homologue of S. cerevisiae Sla2p, interacts with membrane-associated huntingtin in the brain. Nat Genet 16(1):44-53
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
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