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Unusual properties of the fungal conventional kinesin neck domain from Neurospora crassa
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Kallipolitou A, Deluca D, Majdic U, Lakamper S, Cross R, Meyhofer E, Moroder L, Schliwa M, Woehlke G: Unusual properties of the fungal conventional kinesin neck domain from Neurospora crassa. EMBO J 2001, 20:6226-6235.
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(2001)
EMBO J
, vol.20
, pp. 6226-6235
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Kallipolitou, A.1
Deluca, D.2
Majdic, U.3
Lakamper, S.4
Cross, R.5
Meyhofer, E.6
Moroder, L.7
Schliwa, M.8
Woehlke, G.9
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42
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0037415729
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A conserved tyrosine in the neck of a fungal kinesin regulates the catalytic motor core
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Schafer F, Deluca D, Majdic U, Kirchner J, Schliwa M, Moroder L, Woehlke G: A conserved tyrosine in the neck of a fungal kinesin regulates the catalytic motor core. EMBO J 2003, 22:450-458. A mutagenesis approach has been used to study the role of the fungal kinesin neck for motor function. This work focuses on the tyrosine 362 residue that is strictly conserved among fungal kinesins but not present in animal kinesins. The data suggest that a direct interaction of the aromatic ring of Tyr 362 with the head may be responsible for the inhibitory effect of the neck domain on the motor core.
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(2003)
EMBO J
, vol.22
, pp. 450-458
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Schafer, F.1
Deluca, D.2
Majdic, U.3
Kirchner, J.4
Schliwa, M.5
Moroder, L.6
Woehlke, G.7
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43
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0030831244
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The bimC family of kinesins: Essential bipolar mitotic motors driving centrosome separation
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Kashina AS, Rogers GC, Scholey JM: The bimC family of kinesins: essential bipolar mitotic motors driving centrosome separation. Biochim Biophys Acta 1997, 1357:257-271.
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(1997)
Biochim Biophys Acta
, vol.1357
, pp. 257-271
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Kashina, A.S.1
Rogers, G.C.2
Scholey, J.M.3
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44
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0035171581
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Gamma-tubulin and the C-terminal motor domain kinesin-like protein, KLPA, function in the establishment of spindle bipolarity in Aspergillus nidulans
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Prigozhina NL, Walker RA, Oakley CE, Oakley BR: Gamma-tubulin and the C-terminal motor domain kinesin-like protein, KLPA, function in the establishment of spindle bipolarity in Aspergillus nidulans. Mol Biol Cell 2001, 12:3161-3174.
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(2001)
Mol Biol Cell
, vol.12
, pp. 3161-3174
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Prigozhina, N.L.1
Walker, R.A.2
Oakley, C.E.3
Oakley, B.R.4
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45
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0036402582
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csmA, a gene encoding a class V chitin synthase with a myosin motor-like domain of Aspergillus nidulans, is translated as a single polypeptide and regulated in response to osmotic conditions
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Takeshita N, Ohta A, Horiuchi H: csmA, a gene encoding a class V chitin synthase with a myosin motor-like domain of Aspergillus nidulans, is translated as a single polypeptide and regulated in response to osmotic conditions. Biochem Biophys Res Commun 2002, 298:103-109. Filamentous fungi contain a novel gene that encodes a polypeptide with an amino-terminal myosin motor-like domain and a carboxy-terminal chitin synthase domain. In A. nidulans, the null mutant for this gene, csmA, is defective in polarized growth, hyphal wall integrity and conidiophore formation. The csmA null mutant is sensitive to low osmotic conditions. In this work, the authors show that the entire coding region of csmA is translated as a single polypeptide whose level is significantly reduced under high osmotic conditions. This suggests that csmA may play an important role in supporting normal growth under low osmotic conditions.
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(2002)
Biochem Biophys Res Commun
, vol.298
, pp. 103-109
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Takeshita, N.1
Ohta, A.2
Horiuchi, H.3
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47
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0035979251
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Myosin I mutants with only 1% of wild-type actin-activated MgATPase activity retain essential in vivo function(s)
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Liu X, Osherov N, Yamashita R, Brzeska H, Korn ED, May GS: Myosin I mutants with only 1% of wild-type actin-activated MgATPase activity retain essential in vivo function(s). Proc Natl Acad Sci USA 2001, 98:9122-9127.
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(2001)
Proc Natl Acad Sci USA
, vol.98
, pp. 9122-9127
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Liu, X.1
Osherov, N.2
Yamashita, R.3
Brzeska, H.4
Korn, E.D.5
May, G.S.6
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48
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0036547906
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Myosin I is required for hypha formation in Candida albicans
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Oberholzer U, Marcil A, Leberer E, Thomas DY, Whiteway M: Myosin I is required for hypha formation in Candida albicans. Eukaryot Cell 2002, 1:213-228. In C. albicans, GFP-labeled-Myosin I (CaMyo5) localizes to cortical actin patches at the bud and hyphal tips. A CaMyo5 deletion mutant is viable but cannot form hyphae under hypha-inducing conditions. It exhibits a higher frequency of random budding and a depolarized distribution of cortical actin patches. Mutation of serine 366 to alanine in the 'TEDS-rule' phosphorylation site gives rise to the null mutant phenotype. A S366D mutation, which mimics a phosphorylated serine, allows hypha formation, although it still causes a depolarized distribution of cortical actin patches at the bud and in the majority of the hyphae, suggesting that polarized cortical actin patches may not be essential for hyphal growth.
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(2002)
Eukaryot Cell
, vol.1
, pp. 213-228
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Oberholzer, U.1
Marcil, A.2
Leberer, E.3
Thomas, D.Y.4
Whiteway, M.5
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49
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0037458151
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MYO2 is not essential for viability, but is required for polarized growth and dimorphic switches in Candida albicans
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Woo M, Lee K, Song K: MYO2 is not essential for viability, but is required for polarized growth and dimorphic switches in Candida albicans. FEMS Microbiol Lett 2003, 218:195-202. In C. albicans, the class V myosin is encoded by CaMYO2. CaMYO2 deletion mutants are viable; however, the proliferation of CaMYO2 mutant cells is dramatically decreased. The mutants exhibit defects in the assembly and polarized localization of F-actin and show abnormalities in nuclear shape and migration. The mutants also failed to form germ tubes.
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(2003)
FEMS Microbiol Lett
, vol.218
, pp. 195-202
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Woo, M.1
Lee, K.2
Song, K.3
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50
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0042971415
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TINA interacts with the NIMA kinase in Aspergillus nidulans and negatively regulates astral microtubules during metaphase arrest
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Osmani AH, Davies J, Oakley CE, Oakley BR, Osmani SA: TINA interacts with the NIMA kinase in Aspergillus nidulans and negatively regulates astral microtubules during metaphase arrest. Mol Biol Cell 2003, 14:3169-3179. TinA encodes a protein that interacts with the NIMA mitotic protein kinase in the yeast two hybrid system. TINA is localized to the spindle pole bodies only during mitosis. Deletion of tina displays synthetic lethality with the anaphase-promoting complex/cyclosome mutation bimE7. At the bimE7 metaphase arrest point, few astral microtubules can be observed to emanate from the spindle poles. Interestingly, lack of TINA in the bimE7 background produces a dramatic enhancement of astral microtubules, which often interact to form spindles joined in series. These results suggest that TINA is involved in negative regulation of the astral microtubule organization during metaphase.
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(2003)
Mol Biol Cell
, vol.14
, pp. 3169-3179
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Osmani, A.H.1
Davies, J.2
Oakley, C.E.3
Oakley, B.R.4
Osmani, S.A.5
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51
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0031947483
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The role of the dynactin complex in intracellular motility
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Holleran EA, Karki S, Holzbaur EL: The role of the dynactin complex in intracellular motility. Int Rev Cytol 1998, 182:69-109.
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(1998)
Int Rev Cytol
, vol.182
, pp. 69-109
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Holleran, E.A.1
Karki, S.2
Holzbaur, E.L.3
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52
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0032728976
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Analysis of dynactin subcomplexes reveals a novel actin-related protein associated with the Arp1 minifilament pointed end
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Eckley DM, Gill SR, Melkonian KA, Bingham JB, Goodson HV, Heuser JE, Schroer TA: Analysis of dynactin subcomplexes reveals a novel actin-related protein associated with the Arp1 minifilament pointed end. J Cell Biol 1999, 147:307-320.
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(1999)
J Cell Biol
, vol.147
, pp. 307-320
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Eckley, D.M.1
Gill, S.R.2
Melkonian, K.A.3
Bingham, J.B.4
Goodson, H.V.5
Heuser, J.E.6
Schroer, T.A.7
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53
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0034677929
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The dynein microtubule motor
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King SM: The dynein microtubule motor. Biochim Biophys Acta 2000, 1496:60-75.
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(2000)
Biochim Biophys Acta
, vol.1496
, pp. 60-75
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King, S.M.1
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54
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0034693225
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Light intermediate chain 1 defines a functional subfraction of cytoplasmic dynein which binds to pericentrin
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Tynan SH, Purohit A, Doxsey SJ, Vallee RB: Light intermediate chain 1 defines a functional subfraction of cytoplasmic dynein which binds to pericentrin. J Biol Chem 2000, 275:32763-32768.
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(2000)
J Biol Chem
, vol.275
, pp. 32763-32768
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Tynan, S.H.1
Purohit, A.2
Doxsey, S.J.3
Vallee, R.B.4
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