SPC110/YDR356W Literature Guide Help

Other names published for SPC110: XCM1, NUF1, YDR356W

SPC110 - Protein-protein Interactions (23)

ReferenceOther Genes Addressed
Erlemann S, et al.  (2012) An extended gamma-tubulin ring functions as a stable platform in microtubule nucleation. J Cell Biol 197(1):59-74
Bertazzi DT, et al.  (2011) The cortical protein Lte1 promotes mitotic exit by inhibiting the spindle position checkpoint kinase Kin4. J Cell Biol 193(6):1033-48
Bloom J, et al.  (2011) Global analysis of cdc14 phosphatase reveals diverse roles in mitotic processes. J Biol Chem 286(7):5434-45
Lin TC, et al.  (2011) Phosphorylation of the Yeast gamma-Tubulin Tub4 Regulates Microtubule Function. PLoS One 6(5):e19700
Kollman JM, et al.  (2010) Microtubule nucleating gamma-TuSC assembles structures with 13-fold microtubule-like symmetry. Nature 466(7308):879-82
Kollman JM, et al.  (2008) The Structure of the {gamma}-Tubulin Small Complex: Implications of Its Architecture and Flexibility for Microtubule Nucleation. Mol Biol Cell 19(1):207-15
Neuber A, et al.  (2008) Nuclear export receptor Xpo1/Crm1 is physically and functionally linked to the spindle pole body in budding yeast. Mol Cell Biol 28(17):5348-58
Muller EG, et al.  (2005) The organization of the core proteins of the yeast spindle pole body. Mol Biol Cell 16(7):3341-52
Niepel M, et al.  (2005) The nuclear pore complex-associated protein, Mlp2p, binds to the yeast spindle pole body and promotes its efficient assembly. J Cell Biol 170(2):225-35
Okano H, et al.  (2004) A novel mechanism of intragenic complementation between Phe to Ala calmodulin mutations. J Biochem 135(3):289-95
Okano H and Ohya Y  (2003) Binding of calmodulin to Nuf1p is required for karyogamy in Saccharomyces cerevisiae. Mol Genet Genomics 269(5):649-57
Vinh DB, et al.  (2002) Reconstitution and characterization of budding yeast gamma-tubulin complex. Mol Biol Cell 13(4):1144-57
Friedman DB, et al.  (2001) Yeast Mps1p phosphorylates the spindle pole component Spc110p in the N-terminal domain. J Biol Chem 276(21):17958-67
Elliott S, et al.  (1999) Spc29p is a component of the Spc110p subcomplex and is essential for spindle pole body duplication. Proc Natl Acad Sci U S A 96(11):6205-10
Nguyen T, et al.  (1998) A genetic analysis of interactions with Spc110p reveals distinct functions of Spc97p and Spc98p, components of the yeast gamma-tubulin complex. Mol Biol Cell 9(8):2201-16
Knop M and Schiebel E  (1997) Spc98p and Spc97p of the yeast gamma-tubulin complex mediate binding to the spindle pole body via their interaction with Spc110p. EMBO J 16(23):6985-95
Geier BM, et al.  (1996) Binding of centrins and yeast calmodulin to synthetic peptides corresponding to binding sites in the spindle pole body components Kar1p and Spc110p. J Biol Chem 271(45):28366-74
Kilmartin JV and Goh PY  (1996) Spc110p: assembly properties and role in the connection of nuclear microtubules to the yeast spindle pole body. EMBO J 15(17):4592-602
Spang A, et al.  (1996) The spacer protein Spc110p targets calmodulin to the central plaque of the yeast spindle pole body. J Cell Sci 109 ( Pt 9)():2229-37
Stirling DA, et al.  (1996) Mutations which block the binding of calmodulin to Spc110p cause multiple mitotic defects. J Cell Sci 109 ( Pt 6)():1297-310
Spang A, et al.  (1995) The Cdc31p-binding protein Kar1p is a component of the half bridge of the yeast spindle pole body. J Cell Biol 128(5):863-77
Stirling DA, et al.  (1994) Interaction with calmodulin is required for the function of Spc110p, an essential component of the yeast spindle pole body. EMBO J 13(18):4329-42
Geiser JR, et al.  (1993) The essential mitotic target of calmodulin is the 110-kilodalton component of the spindle pole body in Saccharomyces cerevisiae. Mol Cell Biol 13(12):7913-24