Π Π΅Π³ΡΠ»ΡΡΠΈΡ ΡΡΠ°Π½ΡΠΏΠΎΡΡΠ° ΠΌΠΈΡΠΎΡ ΠΎΠ½Π΄ΡΠΈΠΉ Π² ΠΊΠ»Π΅ΡΠΊΠ°Ρ ΠΌΠ»Π΅ΠΊΠΎΠΏΠΈΡΠ°ΡΡΠΈΡ
ΠΠΈΡΡΠ΅ΡΡΠ°ΡΠΈΡ
ΠΠ΅Π»ΠΎΠΊ mDial ΠΈΠ³ΡΠ°Π΅Ρ ΠΊΠ»ΡΡΠ΅Π²ΡΡ ΡΠΎΠ»Ρ Π² ΡΠ΅Π³ΡΠ»ΡΡΠΈΠΈ ΡΡΠ°Π½ΡΠΏΠΎΡΡΠ° ΠΌΠΈΡΠΎΡ ΠΎΠ½Π΄ΡΠΈΠΉ. Π€Π»ΡΠΎΡΠ΅ΡΡΠ΅Π½ΡΠ½Π°Ρ ΠΌΠΈΠΊΡΠΎΡΠΊΠΎΠΏΠΈΡ2. 2. 1. Π€ΠΈΠΊΡΠ°ΡΠΈΡ ΠΊΠ»Π΅ΡΠΎΠΊ. ΠΠΈΠΊΡΠΎΠΈΠ½ΡΠ΅ΠΊΡΠΈΡ2. 5. 1. ΠΠΈΠΊΡΠΎΠΈΠ½ΡΠ΅ΠΊΡΠΈΡ ΠΊΠΠΠ. ΠΠ½ΡΠΈΡΠ΅Π»Π°, ΠΈΡΠΏΠΎΠ»ΡΠ·ΡΠ΅ΠΌΡΠ΅ Π² ΡΠ°Π±ΠΎΡΠ΅. 2. Π ΠΎΠ»Ρ Π±Π΅Π»ΠΊΠΎΠ² ΡΠΎΡΠΌΠΈΠ½ΠΎΠ²ΠΎΠ³ΠΎ ΡΠ΅ΠΌΠ΅ΠΉΡΡΠ²Π° Π² ΠΎΡΠ³Π°Π½ΠΈΠ·Π°ΡΠΈΠΈ Π°ΠΊΡΠΈΠ½ΠΎΠ²ΠΎΠ³ΠΎ ΡΠΈΡΠΎΡΠΊΠ΅Π»Π΅ΡΠ°. ΠΠΠ ΠΊΠΎΠ½ΡΡΡΡΠΊΡΠΈΠΈ. Π ΠΎΠ»Ρ F-Π°ΠΊΡΠΈΠ½Π° Π² ΠΈΠ½Π³ΠΈΠ±ΠΈΡΠΎΠ²Π°Π½ΠΈΠΈ Π΄Π²ΠΈΠΆΠ΅Π½ΠΈΡ ΠΌΠΈΡΠΎΡ ΠΎΠ½Π΄ΡΠΈΠΉ. ΠΠΎΠ»ΠΈΠΌΠ΅ΡΠΈΠ·Π°ΡΠΈΡ Π°ΠΊΡΠΈΠ½Π°, ΡΡΠΈΠΌΡΠ»ΠΈΡΡΠ΅ΠΌΠ°Ρ Π½Π΅Π·Π°Π²ΠΈΡΠΈΠΌΡΠΌΠΈ ΠΎΡ mDial… Π§ΠΈΡΠ°ΡΡ Π΅ΡΡ >
- Π‘ΠΎΠ΄Π΅ΡΠΆΠ°Π½ΠΈΠ΅
- ΠΡΠ΄Π΅ΡΠΆΠΊΠ°
- ΠΠΈΡΠ΅ΡΠ°ΡΡΡΠ°
- ΠΡΡΠ³ΠΈΠ΅ ΡΠ°Π±ΠΎΡΡ
- ΠΠΎΠΌΠΎΡΡ Π² Π½Π°ΠΏΠΈΡΠ°Π½ΠΈΠΈ
Π‘ΠΎΠ΄Π΅ΡΠΆΠ°Π½ΠΈΠ΅
- Π‘ΠΠΠ‘ΠΠ ΠΠ ΠΠΠ―Π’Π«Π₯ Π‘ΠΠΠ ΠΠ©ΠΠΠΠ
- ΠΠ»Π°Π²Π° 1. ΠΠΠΠΠ ΠΠΠΠΠ«Π₯ ΠΠΠ’ΠΠ ΠΠ’Π£Π Π«
- 1. 1. Π Π°ΡΠΏΡΠ΅Π΄Π΅Π»Π΅Π½ΠΈΠ΅ ΠΈ ΡΡΠ½ΠΊΡΠΈΠΈ ΠΌΠΈΡΠΎΡ ΠΎΠ½Π΄ΡΠΈΠΉ Π² ΠΊΠ»Π΅ΡΠΊΠ΅
- 1. 2. Π¦ΠΈΡΠΎΡΠΊΠ΅Π»Π΅Ρ, ΠΊΠ°ΠΊ ΡΡΠ΅Π΄ΡΡΠ²ΠΎ Π²Π½ΡΡΡΠΈΠΊΠ»Π΅ΡΠΎΡΠ½ΠΎΠ³ΠΎ ΡΡΠ°Π½ΡΠΏΠΎΡΡΠ°
- 1. 2. 1. ΠΡΠΎΠ±Π΅Π½Π½ΠΎΡΡΠΈ ΡΠΈΡΡΠ΅ΠΌΡ ΠΌΠΈΠΊΡΠΎΡΡΡΠ±ΠΎΡΠ΅ΠΊ
- 1. 2. 2. ΠΡΠΎΠ±Π΅Π½Π½ΠΎΡΡΠΈ Π°ΠΊΡΠΈΠ½ΠΎΠ²ΠΎΠ³ΠΎ ΡΠΈΡΠΎΡΠΊΠ΅Π»Π΅ΡΠ°
- 1. 2. 2. 1. ΠΠΎΠ»ΠΈΠΌΠ΅ΡΠΈΠ·Π°ΡΠΈΡ Π½ΠΎΠ²ΡΡ Π°ΠΊΡΠΈΠ½ΠΎΠ²ΡΡ ΠΌΠΈΠΊΡΠΎΡΠΈΠ»Π°ΠΌΠ΅Π½ΡΠΎΠ². ΠΠ³Ρ2/3-ΠΊΠΎΠΌΠΏΠ»Π΅ΠΊΡ
- 1. 2. 2. 2. Π ΠΎΠ»Ρ Π±Π΅Π»ΠΊΠΎΠ² ΡΠΎΡΠΌΠΈΠ½ΠΎΠ²ΠΎΠ³ΠΎ ΡΠ΅ΠΌΠ΅ΠΉΡΡΠ²Π° Π² ΠΎΡΠ³Π°Π½ΠΈΠ·Π°ΡΠΈΠΈ Π°ΠΊΡΠΈΠ½ΠΎΠ²ΠΎΠ³ΠΎ ΡΠΈΡΠΎΡΠΊΠ΅Π»Π΅ΡΠ°
- 1. 2. 3. Π Π΅Π³ΡΠ»ΡΡΠΈΡ Π²Π½ΡΡΡΠΈΠΊΠ»Π΅ΡΠΎΡΠ½ΠΎΠΉ ΠΎΡΠ³Π°Π½ΠΈΠ·Π°ΡΠΈΠΈ ΠΌΠΈΠΊΡΠΎΡΡΡΠ±ΠΎΡΠ΅ΠΊ ΠΈ Π°ΠΊΡΠΈΠ½ΠΎΠ²ΠΎΠ³ΠΎ ΡΠΈΡΠΎΡΠΊΠ΅Π»Π΅ΡΠ°
- 1. 2. 4. Π£ΡΠ°ΡΡΠΈΠ΅ Π΄Π²ΡΡ ΡΠΈΡΠΎΡΠΊΠ΅Π»Π΅ΡΠ½ΡΡ ΡΠΈΡΡΠ΅ΠΌ Π² ΡΡΠ°Π½ΡΠΏΠΎΡΡΠ΅ ΠΌΠΈΡΠΎΡ ΠΎΠ½Π΄ΡΠΈΠΉ
- 1. 3. ΠΠΎΠ»Π΅ΠΊΡΠ»ΡΡΠ½ΡΠ΅ ΠΌΠΎΡΠΎΡΡ, ΡΡΠ°ΡΡΠ²ΡΡΡΠΈΠ΅ Π² Π΄Π²ΠΈΠΆΠ΅Π½ΠΈΠΈ ΠΌΠΈΡΠΎΡ ΠΎΠ½Π΄ΡΠΈΠΉ
- 1. 4. Π Π΅Π³ΡΠ»ΡΡΠΈΡ ΡΠ°ΡΠΏΡΠ΅Π΄Π΅Π»Π΅Π½ΠΈΡ ΠΌΠΈΡΠΎΡ ΠΎΠ½Π΄ΡΠΈΠΉ ΠΊΠ°ΠΊ ΠΏΡΠΎΡΠ΅ΡΡ ΠΏΠ΅ΡΠ΅ΠΊΠ»ΡΡΠ΅Π½ΠΈΡ ΠΌΠ΅ΠΆΠ΄Ρ ΡΡΠ°ΡΠΈΠΎΠ½Π°ΡΠ½ΡΠΌ ΠΈ ΠΏΠΎΠ΄Π²ΠΈΠΆΠ½ΡΠΌ ΡΠΎΡΡΠΎΡΠ½ΠΈΡΠΌΠΈ
- 1. 5. ΠΠΈΠ΄Π΅ΠΎΠΌΠΈΠΊΡΠΎΡΠΊΠΎΠΏΠΈΡΠ΅ΡΠΊΠΈΠ΅ ΠΏΠΎΠ΄Ρ ΠΎΠ΄Ρ ΠΊ Π½Π°Π±Π»ΡΠ΄Π΅Π½ΠΈΡ ΠΌΠΈΡΠΎΡ ΠΎΠ½Π΄ΡΠΈΠΉ Π² ΠΆΠΈΠ²ΡΡ ΠΊΠ»Π΅ΡΠΊΠ°Ρ
- ΠΠ»Π°Π²Π° 2. ΠΠΠ’ΠΠ ΠΠΠΠ« Π ΠΠΠ’ΠΠΠ«
- 2. 1. ΠΡΠ»ΡΡΠΈΠ²ΠΈΡΠΎΠ²Π°Π½ΠΈΠ΅ ΠΊΠ»Π΅ΡΠΎΠΊ
- 2. 2. Π€Π»ΡΠΎΡΠ΅ΡΡΠ΅Π½ΡΠ½Π°Ρ ΠΌΠΈΠΊΡΠΎΡΠΊΠΎΠΏΠΈΡ
- 2. 2. 1. Π€ΠΈΠΊΡΠ°ΡΠΈΡ ΠΊΠ»Π΅ΡΠΎΠΊ
- 2. 2. 2. ΠΡΠΎΡΠ΅Π΄ΡΡΠ° ΠΈΠΌΠΌΡΠ½ΠΎΡΠ»ΡΠΎΡΠ΅ΡΡΠ΅Π½ΡΠ½ΠΎΠ³ΠΎ ΠΎΠΊΡΠ°ΡΠΈΠ²Π°Π½ΠΈΡ
- 2. 2. 3. ΠΠ½ΡΠΈΡΠ΅Π»Π°, ΠΈΡΠΏΠΎΠ»ΡΠ·ΡΠ΅ΠΌΡΠ΅ Π² ΡΠ°Π±ΠΎΡΠ΅
- 2. 2. 4. ΠΠΊΡΠ°ΡΠΈΠ²Π°Π½ΠΈΠ΅ Π°ΠΊΡΠΈΠ½Π°
- 2. 3. ΠΠΠ ΠΊΠΎΠ½ΡΡΡΡΠΊΡΠΈΠΈ
- 2. 4. Π’ΡΠ°Π½ΡΡΠ΅ΠΊΡΠΈΡ ΠΊΠ»Π΅ΡΠΎΠΊ
- 2. 5. ΠΠΈΠΊΡΠΎΠΈΠ½ΡΠ΅ΠΊΡΠΈΡ
- 2. 5. 1. ΠΠΈΠΊΡΠΎΠΈΠ½ΡΠ΅ΠΊΡΠΈΡ ΠΊΠΠΠ
- 2. 5. 2. ΠΠΈΠΊΡΠΎΠΈΠ½ΡΠ΅ΠΊΡΠΈΡ Π±Π΅Π»ΠΊΠ°
- 2. 6. ΠΠΎΠ»ΡΡΠ΅Π½ΠΈΠ΅ Π²ΠΈΠ΄Π΅ΠΎΠΌΠΈΠΊΡΠΎΡΠΊΠΎΠΏΠΈΡΠ΅ΡΠΊΠΈΡ Π΄Π°Π½Π½ΡΡ
- 2. 7. ΠΠ±ΡΠ°Π±ΠΎΡΠΊΠ° Π΄Π°Π½Π½ΡΡ
- ΠΠ»Π°Π²Π° 3. Π ΠΠΠ£ΠΠ¬Π’ΠΠ’Π« ΠΠ‘Π‘ΠΠΠΠΠΠΠΠΠ―
- 3. 1. ΠΠ°Π±Π»ΡΠ΄Π΅Π½ΠΈΠ΅ ΠΌΠΈΡΠΎΡ ΠΎΠ½Π΄ΡΠΈΠΉ Π² ΠΆΠΈΠ²ΡΡ ΠΊΠ»Π΅ΡΠΊΠ°Ρ
- 3. 2. ΠΠΏΡΠ΅Π΄Π΅Π»Π΅Π½ΠΈΠ΅ ΠΏΠΎΠ΄Π²ΠΈΠΆΠ½ΠΎΡΡΠΈ ΠΌΠΈΡΠΎΡ ΠΎΠ½Π΄ΡΠΈΠΉ ΠΊΠ»Π΅ΡΠΊΠ°Ρ
- 3. 3. ΠΠΎΠ΄Π²ΠΈΠΆΠ½ΠΎΡΡΡ ΠΌΠΈΡΠΎΡ ΠΎΠ½Π΄ΡΠΈΠΉ Π½Π°Ρ ΠΎΠ΄ΠΈΡΡΡ ΠΏΠΎΠ΄ ΠΊΠΎΠ½ΡΡΠΎΠ»Π΅ΠΌ Π²Π½Π΅ΡΠ½ΠΈΡ ΡΠ°ΠΊΡΠΎΡΠΎΠ²
- 3. 4. ΠΠΈΠ·ΠΎΡΠΎΡΡΠ°ΡΠΈΠ΄Π½Π°Ρ ΠΊΠΈΡΠ»ΠΎΡΠ° ΠΈΠ½Π³ΠΈΠ±ΠΈΡΡΠ΅Ρ ΠΏΠΎΠ΄Π²ΠΈΠΆΠ½ΠΎΡΡΡ ΠΌΠΈΡΠΎΡ ΠΎΠ½Π΄ΡΠΈΠΉ ΡΠ΅ΡΠ΅Π· Π±Π΅Π»ΠΎΠΊ RhoA
- 3. 5. ΠΠ΅Π»ΠΎΠΊ RhoA ΡΠ΅Π³ΡΠ»ΠΈΡΡΠ΅Ρ ΡΠ°ΡΠΏΡΠ΅Π΄Π΅Π»Π΅Π½ΠΈΠ΅ ΠΌΠΈΡΠΎΡ
ΠΎΠ½Π΄ΡΠΈΠΉ, Π΄Π΅ΠΉΡΡΠ²ΡΡ ΡΠ΅ΡΠ΅Π· ΡΠ²ΠΎΠΈ Π±Π΅Π»ΠΊΠΈ-ΠΌΠΈΡΠ΅Π½ΠΈ
- 3. 5. 1. ΠΠ·ΠΌΠ΅Π½Π΅Π½ΠΈΠ΅ Π°ΠΊΡΠΈΠ²Π½ΠΎΡΡΠΈ Rho ΠΊΠΈΠ½Π°Π·Ρ Π½Π΅ Π²Π»ΠΈΡΠ΅Ρ Π½Π° ΠΏΠΎΠ΄Π²ΠΈΠΆΠ½ΠΎΡΡΡ ΠΌΠΈΡΠΎΡ ΠΎΠ½Π΄ΡΠΈΠΉ
- 3. 5. 2. ΠΠ΅Π»ΠΎΠΊ mDial ΠΈΠ³ΡΠ°Π΅Ρ ΠΊΠ»ΡΡΠ΅Π²ΡΡ ΡΠΎΠ»Ρ Π² ΡΠ΅Π³ΡΠ»ΡΡΠΈΠΈ ΡΡΠ°Π½ΡΠΏΠΎΡΡΠ° ΠΌΠΈΡΠΎΡ ΠΎΠ½Π΄ΡΠΈΠΉ
- 3. 6. Π ΠΎΠ»Ρ F-Π°ΠΊΡΠΈΠ½Π° Π² ΠΈΠ½Π³ΠΈΠ±ΠΈΡΠΎΠ²Π°Π½ΠΈΠΈ Π΄Π²ΠΈΠΆΠ΅Π½ΠΈΡ ΠΌΠΈΡΠΎΡ ΠΎΠ½Π΄ΡΠΈΠΉ
- 3. 7. ΠΠΎΠ»ΠΈΠΌΠ΅ΡΠΈΠ·Π°ΡΠΈΡ Π°ΠΊΡΠΈΠ½Π°, ΡΡΠΈΠΌΡΠ»ΠΈΡΡΠ΅ΠΌΠ°Ρ Π½Π΅Π·Π°Π²ΠΈΡΠΈΠΌΡΠΌΠΈ ΠΎΡ mDial ΡΠΏΠΎΡΠΎΠ±Π°ΠΌΠΈ, Π½Π΅ ΡΠ½ΠΈΠΆΠ°Π΅Ρ ΠΏΠΎΠ΄Π²ΠΈΠΆΠ½ΠΎΡΡΡ ΠΌΠΈΡΠΎΡ ΠΎΠ½Π΄ΡΠΈΠΉ
- ΠΠ»Π°Π²Π° 4. ΠΠΠ‘Π£ΠΠΠΠΠΠ Π ΠΠΠ£ΠΠ¬Π’ΠΠ’ΠΠ
- ΠΠ«ΠΠΠΠ«
Π‘ΠΏΠΈΡΠΎΠΊ Π»ΠΈΡΠ΅ΡΠ°ΡΡΡΡ
- Alberts A.S. (2001). Identification of a carboxyl-terminal diaphanous-related formin homology protein autoregulatory domain. J Biol Chem 276, 2824−2830.
- Allen R.D., Metuzals J., Tasaki I., Brady S.T., Gilbert S.P. (1982). Fast axonal transport in squid giant axon. Science 218, 1127−1129
- Amano M., Chihara K., Kimura K., Fukata Y., Nakamura N., Matsuura Y., Kaibuchi K. (1997). Formation of actin stress fibers and focal adhesions enhanced by Rho-kinase. Science 75, 1308−1311.
- Andersen S.S. (2000). Spindle assembly and the art of regulating microtubule dynamics by MAPs and stathmin/Opl8. Trends Cell Biol. 10, 261−267.
- Aniento F., Emans N., Griffiths G., Gruenberg J. (1993). Cytoplasmic dynein-dependent vesicular transport from early to late endosomes. J. Cell Biol., 123, 1373−1387.
- Arrieumerlou C., Donnadieu E., Brennan P., Keryer G., Bismuth G., Cantrell D., Trautmann A. (1998). Involvement of phosphoinositide 3-kinase and Rac in membrane ruffling induced by IL-2 in T cells. Eur J Immunol 28, 1877−1885.
- Barkalow K., Hamasaki Π’., Satir P. (1994). Regulation of 22S dynein by a 29kD light chain. J Cell Biol 126, 727−735
- Baumann O, Murphy D.B. (1995). Microtubule-associated movement of mitochondria and small particles in Acanthamoeba castellanii. Cell Motil Cytoskeleton. 32 (4): 305−17.
- Bereiter-Hahn J. (1976). Dimethylaminostyrylmethylpyridiniumiodine (daspmi) as a fluorescent probe for mitochondria in situ. Biochim Biophys Acta. Jan 15- 423(1): 1−14.
- Berg J.S., Powell B.C., Cheney R.E. (2001). A millennial myosin census. Mol Biol Cell Apr 12:4 780−94
- Bradley T.J., Satir P. (1979). Evidence of microfilament-associated mitochondrial movement. J Supramol Struct. 12(2): 165−75.
- Brady S.T., Lasek R.J., Allen R.D. (1982). Fast axonal transport in extruded axoplasm from squid giant axon. Science 218, 1129−1131
- Brenner C, Kroemer G. (2000). Apoptosis. Mitochondria—the death signal integrators. Science. Aug 18- 289(5482): 1150−1.
- Bubb M.R., Senderowicz A.M.J., Sausville E.A., Duncan K.L.K., Korn E.D. (1994). Jasplakinolide, a cytotoxic natural product, induces actin polymerization and competitively inhibits the binding of phalloidin to F-actin. J. Biol. Chem. 269, 14 869−14 871
- Cambray-Deakin M.A., Robson S.J., Burgoyne R.D. (1988). Colocalisation of acetylated microtubules, glial filaments, and mitochondria in astrocytes in vitro. Cell Motil Cytoskeleton. 10(3): 438−49.
- Carlier M.F. and Pantaloni D. (1997). Control of actin dynamics in cell motility. J. Mol. Biol. 269, 459−467.
- Castrillon D.H. and Wasserman S.A. (1994). Diaphanous is required for cytokinesis in Drosophila and shares domains of similarity with the productsof the limb deformity gene. Development 120, 3367−3377.
- Chada S.R. and Hollenbeck P.J. (2003). Mitochondrial movement and positioning in axons: the role of growth factor signaling. J Exp Biol 206, 19 851 992.
- Chada S.R. and Hollenbeck P.J. (2004). Nerve Growth Factor Signaling Regulates Motility and Docking of Axonal Mitochondria. Current Biol. 14, 1272−1276.
- Chang F., Drubin D., Nurse P. (1997). cdcl2p, a protein required for cytokinesis in fission yeast, is a component of the cell division ring and interacts with profilin. J. Cell Biol. 137, 169−182.
- Chilcote T.J. and Johnson K.A. (1990). Phosphorylation of Tetrahymena 22 S dynein. J Biol Chem 265, 17 257−17 266
- Collins T.J., Berridge M.J., Lipp P., Bootman M.D. (2002). Mitochondria are morphologically and functionally heterogenous within cells. EMBO J., 21, 16 161 627.
- Cook T.A., Nagasaki Π’., Gundersen G.G. (1998). Rho guanosine triphosphatase mediated the selective stabilization of microtubules induced by lysophosphatidic acid. J Cell Biol, 141:175−185.
- Copeland J.W. and Treisman R. (2002). The Diaphanous-related formin mDial controls serum response factor activity through its effects on actin polymerization. Mol. Biol. Cell 13, 4088−4099.
- Corthesy-Theulaz I., Pauloin A., Pfeffer S.R. (1992). Cytoplasmicdynein participates in the centrosomal localization of the Golgi complex. J. Cell Biol., 118, 1333−1345.
- Cossarizza A., Salvioli S. (2001). Analysis of mitochondria during cell death. Methods Cell Biol. 63: 467−86
- Csordas G., Thomas A.P., Hajnoczky G. (1999). Quasi-synaptic calcium signal transmission between endoplasmic reticulum and mitochondria. EMBOJ. 18:96−108.
- De Vos K.J., Sable J., Miller K.E., Sheetz M.P. (2003). Expression of phosphatidylinositol (4,5) bisphosphate-specific pleckstrin homology domains alters direction but not the level of axonal transport of mitochondria. Mol. Biol. Cell 14, 3636−3649.
- De Vos K., Severin F., Van Herreweghe F., Vancompernolle K., Goossens V., Hyman A., Grooten J. (2000). Tumor necrosis factor receptor induces hyperphosphorylation of kinesin light chain and inhibits transport of mitochondria. J.Cell.Biol. 149:1207−1214.
- De Zwaan T.M., Ellingson E., Pellman D., Roof D.M. (1997). Kinesin-related KIP3 of Saccharomyces cerevisiae is required for a distinct step in nuclear migration. J Cell Biol. Sep 8−138(5):1023−40.
- Del Pozo M.A., Alderson N.B., Kiosses W.B., Chiang H.H., Anderson R.G., Schwartz M.A. (2004). Integrins regulate rac targeting by internalization of membrane domains. Science 303, 839−842.
- Desagher S., Martinou J.C. (2000). Mitochondria as the central control point of apoptosis. Trends Cell Biol. Sep-10(9):369−77. Review.
- Dillman J.F. and Pfister K.K. (1994). Differential phosphorylation in vivo of cytoplasmic dynein associated with anterogradely moving organelles. J Cell Biol 127, 1671−1681.
- Elluru R.G., Bloom G.S., Brady S.T. (1995). Fast axonal transport of kinesin in the rat visual system: functionality of kinesin heavy chain isoforms. Mol Biol Cell. 1995 Jan-6(l):21−40. Erratum in: Mol Biol Cell Sep- 6(9): 1261.
- Etienne-Manneville S. and Hall A. (2001). Integrin-mediated activation of Cdc42 controls cell polarity in migrating astrocytes through PKCzeta. Cell 106, 489−498.
- Etienne-Manneville S. and Hall A. (2002) Rho GTPases in cell biology. Nature. Dec 12−420(6916):629−35. Review.
- Evangelista M., Blundell K., Longtine M.S., Chow C.J., Adames N.,
- Pringle J.R., Peter M., Boone C. (1997). Bnilp, a yeast forminlinking cdc42p and the actin cytoskeleton during polarized morphogenesis.1. Science 276, 118−122.
- Evangelista M., Pruyne D., Amberg D.C., Boone C., Bretscher A. (2002). Formins direct Arp2/3-independent actin filament assembly to polarize cell growth in yeast. Nat. Cell Biol. 4, 32−41.
- Evangelista M., Zigmond S., Boone C. (2003). Formins: signaling effectors for assembly and polarization of actin filaments. J Cell Sci. Jul 1- 116(Pt 13): 260 311. Review.
- Evans L.L. and Bridgman P.C. (1995). Particles move along actin filament bundles in nerve growth cones. Proc Natl Acad Sci USA 92, 10 954−10 958.
- Fath K.R., Trimbur G.M., Burgess D.R. (1994). Molecularmotors are differentially distributed on Golgi membranes from polarizedepithelial cells. J. Cell Biol., 126, 661−675.
- Fernandez-Borja M., Janssen L., Verwoerd D., Hordijk P., Neefjes J. (2005) RhoB regulates endosome transport by promoting actin assembly on endosomal membranes through Dial. J Cell Sci. Jun 15- 118(Pt 12):2661−70.
- Forman D.S., Lynch K.J., Smith R.S. (1987). Organelle dynamics in lobster axons: anterograde, retrograde and stationary mitochondria. Brain Res 412, 96 106.
- Gasman S., Kalaidzidis Y., Zerial M. (2003). RhoD regulates endosome dynamics through Diaphanous-related Formin and Src tyrosine kinase. Nat Cell Biol. Mar- 5(3): 195−204. Erratum in: Nat Cell Biol. Jul- 5(7): 680.
- Goldstein L.S. (2001). Kinesin molecular motors: transport pathways, receptors, and human disease. Proc Natl Acad Sci USA. Jun 19- 98(13): 6999−7003. Review.
- Goldstein L.S. and Gunawardena S. (2000). Flying through the drosophila cytoskeletal genome. J. Cell Biol. 150, F63−68.
- Hall A. (1998). Rho GTPases and the actin cytoskeleton. Science. 279:509−514.
- Harlander R.S., Way M., Ren Q., Howe D., Grieshaber S.S., Heinzen R.A. (2003). Effects of ectopically expressed neuronal Wiskott-Aldrich syndrome protein domains on Rickettsia rickettsii actin-based motility. Infect Immun. V. 71(3). P. 1551−6.
- Higgs H.N. and Pollard T.D. (2001). Regulation of actin filament network formation through Arp2/3 complex: activation by a diverse array of proteins. Annu. Rev. Biochem. 70, 649−676
- Hirokawa N., Sato-Yoshitake R., Yoshida Π’., Kawashima T. (1990). Brain dynein (MAP 1Π‘) localizes on both anterogradely and retrogradely transported membranous organelles in vivo. J Cell Biol. Sep- 111(3): 1027−37.
- Hirokawa N. (1998). Kinesin and dynein superfamily proteins and the mechanism of organelle transport. Science 279, 519−526.
- Holleran E.A., Tokito M.K., Karki S., Holzbaur E.L.F. (1996). Centractin (ARP1) associates with spectrin revealing a potential mechanism to link dynactin to intracellular organelles. J. Cell Biol., 135, 1815−1829.
- Holzbaur E.L., Vallee RB. (1994). DYNEINS: molecular structure and cellular function. Annu Rev Cell Biol. 10: 339−72. Review.
- Hotani H., Horio T. (1988). Dynamics of microtubules visualized by darkfield microscopy: treadmilling and dynamic instability. Cell Motil Cytoskeleton 10:12 229−36.
- Johnson L.V., Walsh M.L., Chen L.B. (1980) «Localization of mitochondria in living cells with rhodamine 123.» Proc Natl Acad Sci USA 77, 990−994 PN774.
- Kelleher J.F., Atkinson S.J., Pollard T.D. (1995). Sequences, structural models, and cellular localization of the actin-related proteins Arp2 and Arp3 from Acanthamoeba. J Cell Biol, 131: 385−397.
- Kimura K., Ito M., Amano M., Chihara K., Fukata Y., Nakafuku M., Yamamori Π., Feng J., Nakano Π’., Okawa K., Iwamatsu A., Kaibuchi K. (1996). Regulation of myosin phosphatase by Rho and Rho-associated kinase (Rho-kinase). Science 273,245−248.
- Z., Okamoto K., Hayashi Y., Sheng M. (2004). The importance of dendritic mitochondria in the morphogenesis and plasticity of spines and synapses. Cell. Dec 17−119(6):873−87.
- Matthies H.J.G., Miller R.J., Palfrey H.C. (1993). Calmodulin binding to and cAMPdependent phosphorylation of kinesin light chains modulate kinesin ATPase activity. J Biol Chem 268, 11 176−11 187.
- Mcllvain J.M., Burkhardt J.K., HammAlvarez S., Argon Y., Sheetz M.P. (1994). Regulation of kinesin activity by phosphorylation of kinesinassociated proteins. J Biol Chem 269, 19 176−19 182.
- Miki H., Miura K., Takenawa T. (1996). N-WASP, a novel actindepolymerizing protein, regulates the cortical cytoskeletal rearrangementin a PIP2-dependent manner downstream of tyrosine kinases. EMBO J. 15, 5326−5335.
- Miki H., Sasaki Π’., Takai Y., Takenawa T. (1998). Induction of filopodium formation by a WASP-related actin-depolymerizing protein N-WASP. Nature 391,93−96.
- Miller K.E., Sheetz M.P. (2004). Axonal mitochondrial transport and potential are correlated. J Cell Sci. Jun 1- 117(Pt 13):2791−804. Epub 2004 May 18.
- Moreau V., Frischknecht F., Reckmann I., Vincentelli R., Rabut G., Stewart D., Way M. (2000). A complex of N-WASP and WIP integrates signalling cascades that lead to actin polymerization. Nature Cell Biol. 2, 441−448.
- Morris R.L. and Hollenbeck P.J. (1993). The regulation of bidirectional mitochondrial transport is coordinated with axonal outgrowth. J Cell Sci 104, 917−927.
- Morris R.L. and Hollenbeck P.J. (1995). Axonal transport of mitochondria along microtubules and Factin in living vertebrate neurons. J Cell Biol 131, 13 151 326.
- Mull ins R.D., Heuser J. A., Pollard T.D. (1998). The interaction of Arp2/3 complex with actin: nucleation high affinity pointed end capping and formation of branching networks of filaments. Proc Natl Acad Sci USA, 95:6181−6186.
- Nangaku M., Sato-Yoshitake R., Okada Y., Noda Y., Takemura R., Yamazaki H., Hirokawa N. (1994). KIF1B, a novel microtubule plus end-directed monomeric motor protein for transport of mitochondria. Cell. 79: 1209−1220.
- Narumiya S. (1996). The small GTPase Rho: cellular functions and signal transduction. J Biochem (Tokyo). Aug 120:2 215−28.
- Nobes C.D., Hall A. (1995). Rho, rac, and cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia. Cell 81, 53.
- Oda H., Stockert R.J., Collins C., Wang H., Novikoff P.M., Satir P., Wolkoff A.W. (1995). Interaction of the microtubule cytoskeleton with endocytic vesicles and cytoplasmic dynein in cultured rat hepatocytes. J. Biol. Chem., 270, 1 524 215 249.
- Overly C.C., Rieff H.I., Hollenbeck P.J. (1996). Organelle motility and metabolism in axons vs dendrites of cultured hippocampal neurons. J Cell Sci 109: 971−980.
- Pacher P. and Hajnoczky G. (2001). Propagation of the apoptotic signal by mitochondrial waves. EMBO J. 20:4107−4121.
- Palazzo A.F., Cook T.A., Alberts A.S., Gundersen G.G. (2001). mDia mediates Rho-regulated formation and orientation of stable microtubules. Nat Cell Biol 3, 723−729.
- Palazzo A.F., Eng C.H., Schlaepfer D.D., Marcantonio E.E., Gundersen G.G. (2004). Localized Stabilization of Microtubules by Integrin- and FAK-Facilitated Rho Signaling. Science 303, 836−839.
- Paterson H.F., Self A. J., Garrett M. D., Just I., Aktories K., Hall, A. (1990). Microinjection of recombinant p21rho induces rapid changes in cell morphology. J. Cell Biol. 111, 1001−1007.
- Pollard T.D. and Beltzner C.C. (2002). Structure and function of the Arp2/3 complex. Curr. Opin. Struct. Biol. 12, 768−774.
- Pollard T.D. Blanchoin L., Mullins R.D. (2000). Molecular mechanisms controlling actin filament dynamics in nonmuscle cells. Annu. Rev. Biophys. Biomol. Struct. 29, 545−576.
- Poot M., Zhang Y.Z., Kramer J.A., Wells K.S., Jones L.J., Hanzel D.K., Lugade A.G., Singer V.L., Haugland R.P. (1996). Analysis of mitochondrial morphology and function with novel fixable fluorescent stains. J Histochem Cytochem. Dec-44(12): 1363−72.
- Provance D.W. Jr., Wei M., Ipe V., Mercer J.A. (1996). Cultured melanocytes from dilute mutant mice exhibit dendritic morphology and altered melanosome distribution. Proc Natl Acad Sci USA. Dec 10- 93(25): 14 554−8.
- Pruyne D., Evangelista M., Yang C., Bi E., Zigmond S., Bretscher A., Boone C. (2002). Role of formins in actin assembly: nucleation and barbed-end association. Science 297, 612−615.
- Reif K., Nobes C.D., Thomas G., Hall A., Cantrell D.A. (1996). Phosphatidylinositol 3-kinase signals activate a selective subset of Rac/Rho-dependent effector pathways. Curr Biol 6, 1445−1455.
- Reilein A.R., Rogers S.L., Tuma M.C., Gelfand V.I. (2001). Regulation of molecular motor proteins. Int Rev Cytol. 204: 179−238. Review.
- Ridley A.J. (1996). Rho: theme and variations. Curr. Biol. 10:1256−1264.
- Ridley A.J. (1999). Stress fibres take shape. Nat. Cell Biol. 1, E64-E66.
- Ridley A.J. and Hall A. (1992). The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibres in response to growth factors. Cell 70, 389−399.
- Ridley A.J., Paterson H.F., Johnston C.L., Diekmann D., Hall A. (1992). The small GTP-binding protein Rac regulates growth factor-induced membrane ruffling. Cell. 70: 401−410.
- Rizzuto R., Brini M., Murgia M., Pozzan T. (1993). Microdomains with high Ca2+ close to IP3-sensitive channels that are sensed by neighboring mitochondria. Science. Oct 29- 262 (5134): 744−7.
- Rizzuto R., Brini M., Pizzo P., Murgia M., Pozzan T. (1995). Chimeric green fluorescent protein as a tool for visualizing subcellular organelles in living cells. Curr. Biol. 5, 635−642.
- Rizzuto R., Pinton P., Carrington W., Fay F.S., Fogarty K.E., Lifshitz L.M., Tuft R.A., Pozzan T. (1998). Close contacts with the endoplasmic1. J ireticulum as determinants of mitochondrial Ca responses. Science. 280: 1763−1766.
- Rogers S. L, Gelfand V.I. (1998). Myosin cooperates with microtubule motors during organelle transport in melanophores. Curr. Biol. 8:161−64
- Rogers S.L., Karcher R.L., Roland J.T., Minin A.A., Steffen W., Gelfand V.I. (1999). Regulation of melanosome movement in the cell cycle by reversible association with myosin V. J Cell Biol. Sep 20- 146(6): 1265−76.
- Rohatgi R., Ma L., Miki H., Lopez M., Kirchhausen Π’., Takenawa Π’., Kirschner M.W. (1999). The interaction between N-WASP and the Arp2/3 complex links Cdc42-dependent signals to actin assembly. Cell. Apr 16−97(2):221−31
- Sagot I., Klee S.K., Pellman D. (2002). Yeast formins regulate cell polarity by controlling the assembly of actin cables. Nat. Cell Biol. 4, 42
- SatoYoshitake R., Yorifuji H., Inagaki M., Hirokawa N. (1992). The phosphorylation of kinesin regulates its binding to synaptic vesicles. J Biol Chem 267, 23 930−23 936.
- Schmidt A., Hall A. (2002). Guanine nucleotide exchange factors for Rho GTPases: turning on the switch. Genes Dev. Jul 1- 16(13): 1587−609. Review.
- Schroer T.A. (1994). Structure, function and regulation of cytoplasmic dynein. Curr Opin Cell Biol. Feb- 6(1): 69−73. Review.
- Schulze E. and Kirschner M. (1988). New features of microtubule behavior observed in vivo. Nature 334: 356−359.
- Sheetz M.P. and Spudich J.A. (1983). Movement of myosin-coated fluorescent beads on actin cables in vitro. Nature. May 5−11- 303 (5912): 31−5.
- Small J.V. (1988). The actin cytoskeleton. Electron Microsc. Rev. 1: 155−174.
- Small, J.V., Rottner, K., Kaverina, I. 1999. Functional design in the actin cytoskeleton. Curr. Opin. Cell Biol. 11: 54−60.
- Stebbings H., Hunt C. (1987). The translocation of mitochondria along insect ovarian microtubules from isolated nutritive tubes: a simple reactivated model. J Cell Sci. Dec- 88 (Pt 5): 641−8.
- Stowers R.S., Megeath L.J., Gorska-Andrzejak J., Meinertzhagen I.A., Schwarz T.L. (2002). Axonal transport of mitochondria to synapses depends on milton, a novel Drosophila protein. Neuron. Dec 19- 36 (6): 1063−77.
- Svitkina T.M., Verkhovsky A.B., Borisy G.G. (1995). Improved procedures for electron microscopic visualization of the cytoskeleton of cultured cells. J Struct Biol. 115:290−303.
- Takenaka Π’., Kawakami Π’., Hikawa N., Gotoh H. ((1990). «Axoplasmic transport of mitochondria in cultured dorsal root ganglion cells.» Brain Res 528, 285−290 PN11071.
- Tanaka Y., Kanai Y., Okada Y., Nonaka S., Takeda S., Harada A., Hirokawa N. (1998). Targeted disruption of mouse conventional kinesin heavy chain, kif5B, results in abnormal perinuclear clustering of mitochondria. Cell 93: 1147−1158.
- Trinczek Π., Ebneth A., Mandelkow E.M., Mandelkow E. (1999). Tau regulates the attachment/detachment but not the speed of motors in microtubule-dependent transport of single vesicles and organelles. J Cell Sci. Jul 112 (Pt 14): 2355−67.
- Vale R.D., Reese T.S., Sheetz M.P. (1985). Identification of a novel force-generating protein, kinesin, involved in microtubule-based motility. Cell. Aug- 42(1): 39−50.
- Van Blerkom J. (1991). Microtubule mediation of cytoplasmic and nuclear maturation during the early stages of resumed mitosis in cultured mouse oocytes. Proc Natl Acad Sci USA 88, 5031−5035.
- Van Aelst L., D’Souza-Schorey C. (1997). Rho GTPases and signaling networks. Genes Dev. Sep 15- 11(18): 2295−322. Review.
- Wade R.H., Chretien D., Job D. (1990). Characterization of microtubule protofilament numbers. How does the surface lattice accommodate? J. Mol. Biol., 212, 775−786.
- Wagner O.I., Lifshitz J., Janmey P.A., Linden M., Mcintosh Π’.Π., Leterrier J.F. (2003). Mechanisms of mitochondria-neurofilament interactions. J Neurosci 23, 9046−9058.
- Wasserman S. (1998). FH proteins as cytoskeletal organizers. Trends Cell Biol. 8, 111−115.
- Watanabe N., Kato Π’., Fujita A., Ishizaki Π’., Narumiya S. (1999). Cooperation between mDial and ROCK in Rho-induced actin reorganization. Nat Cell Biol. Jul- 1(3): 136−43
- Wegner A. (1976). Head to tail polymerization of actin. J Mol Biol Nov 108: 1 139−50
- Welch M.D., Iwamatsu A., Mitchison T.J. (1997a). Actin polymerization is induced by Arp2/3 protein complex at the surface of Listeria monocytogenes. Nature, 385: 265−269.
- Welch M.D., DePace A.H., Verma S., Iwamatsu A., Mitchison T.J. (19 976). The human Arp2/3 complex is composed of evolutionarily conserved subunits and is localized to cellular regions of dynamic actinfilament assembly. J Cell Biol, 138:375−384.
- Welch M.D., Rosenblatt J., Skoble J., Portnoy D.A., Mitchison T.J. (1998). Interaction of human Arp2/3 complex and the Listeria monocytogenes ActA protein in actin filament nucleation. Science 281, 105−108.
- Wells A.L., Lin A.W., Chen L.Q., Safer D., Cain S.M., Hasson Π’., Carragher B.O., Milligan R.A., Sweeney H.L. (1999). Myosin VI is an actin-based motor that moves backwards. Nature 401, 505−508.
- Wittmann Π’., Bokoch G.M., Waterman-Storer C.M. (2003). Regulation of leading edge microtubule and actin dynamics downstream of Racl. J Cell Biol 161,845−851.
- Wittmann Π’., Waterman-Storer C.M. (2001). Cell motility: Can Rho GTPases and microtubules point the way? J Cell Sci. Nov 114: Pt 21 3795−803.
- Wu X., Bowers Π., Rao K., Wei Q., Hammer J.A. (1998). Visualization of melanosome dynamics within wild-type and dilute melanocytes suggests a paradigm for myosin V function In vivo. J Cell Biol. Dec 28 143: 7 1899−918.
- Yaffe M.P., Harata D., Verde F., Edison M., Toda Π’., Nurse P. (1996). Microtubules mediate mitochondrial distribution in fission yeast. Proc. Natl. Acad. Sci. USA. 93: 11 664−11 668.
- Yaffe M.P. (1999). The machinery of mitochondrial inheritance and behavior. Science. Mar 5- 283 (5407): 1493−7. Review.
- Yi M., Weaver D., Hajnoczky G. (2004). Control of mitochondrial motility and distribution by the calcium signal: a homeostatic circuit. J Cell Biol. Nov 22- 167(4): 661−72. Epub 2004 Nov 15.
- Zeller R., Haramis A.G., Zuniga A., McGuigan C., Dono R., Davidson G., Chabanis S., Gibson T. (1999). Formin defines a large family of morphoregulatory genes and functions in establishment of the polarising region. Cell Tissue Res. 296, 85−93.
- Zigmond S.H. (1998). Actin cytoskeleton: the Arp2/3 complex gets to the point. Curr Biol. Sep 10−8(18):R654−7. Review.
- Zielinski B.S., Getchell M.L., Getchell T.V. (1988). Ultrastructural characterisitics of sustentacular cells in control and odoranttreated olfactory mucosae of the salamander. Anat Rec 221, 769−779.