-
1
-
-
84857694339
-
Active maintenance of nuclear actin by importin 9 supports transcription
-
1 Dopie, J., Skarp, K.-P., Rajakylä, E.K., Tanhuanpää, K., Vartiainen, M.K., Active maintenance of nuclear actin by importin 9 supports transcription. Proc Natl Acad Sci U S A 109 (2012), E544–E552.
-
(2012)
Proc Natl Acad Sci U S A
, vol.109
, pp. E544-E552
-
-
Dopie, J.1
Skarp, K.-P.2
Rajakylä, E.K.3
Tanhuanpää, K.4
Vartiainen, M.K.5
-
2
-
-
0242641546
-
Exportin 6: a novel nuclear export receptor that is specific for profilin·actin complexes
-
2 Stüven, T., Hartmann, E., Görlich, D., Exportin 6: a novel nuclear export receptor that is specific for profilin·actin complexes. EMBO J 22 (2003), 5928–5940.
-
(2003)
EMBO J
, vol.22
, pp. 5928-5940
-
-
Stüven, T.1
Hartmann, E.2
Görlich, D.3
-
3
-
-
84903541702
-
Rho, nuclear actin, and actin-binding proteins in the regulation of transcription and gene expression
-
3 Rajakylä, E.K., Vartiainen, M.K., Rho, nuclear actin, and actin-binding proteins in the regulation of transcription and gene expression. Small GTPases, 5, 2014, e27539.
-
(2014)
Small GTPases
, vol.5
, pp. e27539
-
-
Rajakylä, E.K.1
Vartiainen, M.K.2
-
4
-
-
84886314384
-
To be or not to be assembled: progressing into nuclear actin filaments
-
4 Grosse, R., Vartiainen, M.K., To be or not to be assembled: progressing into nuclear actin filaments. Nat Rev Mol Cell Biol 14 (2013), 693–697.
-
(2013)
Nat Rev Mol Cell Biol
, vol.14
, pp. 693-697
-
-
Grosse, R.1
Vartiainen, M.K.2
-
5
-
-
84875456639
-
Visualization of actin filaments and monomers in somatic cell nuclei
-
5 Belin, B.J., Cimini, B.A., Blackburn, E.H., Mullins, R.D., Visualization of actin filaments and monomers in somatic cell nuclei. Mol Biol Cell 24 (2013), 982–994.
-
(2013)
Mol Biol Cell
, vol.24
, pp. 982-994
-
-
Belin, B.J.1
Cimini, B.A.2
Blackburn, E.H.3
Mullins, R.D.4
-
6
-
-
84877742076
-
Nuclear actin network assembly by formins regulates the SRF coactivator MAL
-
6 Baarlink, C., Wang, H., Grosse, R., Nuclear actin network assembly by formins regulates the SRF coactivator MAL. Science 340 (2013), 864–867.
-
(2013)
Science
, vol.340
, pp. 864-867
-
-
Baarlink, C.1
Wang, H.2
Grosse, R.3
-
7
-
-
84928776401
-
Nuclear F-actin formation and reorganization upon cell spreading
-
jbc.M114.627166–11216 By utilizing a novel tool, nuclear actin chromobody, to visualize nuclear actin this study reveals for the first time cell spreading-induced nuclear actin polymerization. The study also characterizes the molecular requirements for the polymerization and links the process to MKL1-SRF activation.
-
7• Plessner, M., Melak, M., Chinchilla, P., Baarlink, C., Grosse, R., Nuclear F-actin formation and reorganization upon cell spreading. J Biol Chem, 290, 2015 jbc.M114.627166–11216 By utilizing a novel tool, nuclear actin chromobody, to visualize nuclear actin this study reveals for the first time cell spreading-induced nuclear actin polymerization. The study also characterizes the molecular requirements for the polymerization and links the process to MKL1-SRF activation.
-
(2015)
J Biol Chem
, vol.290
-
-
Plessner, M.1
Melak, M.2
Chinchilla, P.3
Baarlink, C.4
Grosse, R.5
-
8
-
-
84941927563
-
DNA damage induces nuclear actin filament assembly by formin-2 and Spire-1/2 that promotes efficient DNA repair
-
This study suggests a completely novel function for nuclear actin in the context of DNA damage repair. It also highlights the requirement for nuclear actin filaments in this context and demonstrates novel nuclear roles for specific actin nucleators.
-
8•• Belin, B.J., Lee, T., Mullins, R.D., DNA damage induces nuclear actin filament assembly by formin-2 and Spire-1/2 that promotes efficient DNA repair. Elife, 4, 2015, e07735 This study suggests a completely novel function for nuclear actin in the context of DNA damage repair. It also highlights the requirement for nuclear actin filaments in this context and demonstrates novel nuclear roles for specific actin nucleators.
-
(2015)
Elife
, vol.4
, pp. e07735
-
-
Belin, B.J.1
Lee, T.2
Mullins, R.D.3
-
9
-
-
79959259657
-
Structure of a pentavalent G-actin*MRTF-A complex reveals how G-actin controls nucleocytoplasmic shuttling of a transcriptional coactivator
-
ra40–ra40
-
9 Mouilleron, S., Langer, C.A., Guettler, S., McDonald, N.Q., Treisman, R., Structure of a pentavalent G-actin*MRTF-A complex reveals how G-actin controls nucleocytoplasmic shuttling of a transcriptional coactivator. Sci Signal, 4, 2011 ra40–ra40.
-
(2011)
Sci Signal
, vol.4
-
-
Mouilleron, S.1
Langer, C.A.2
Guettler, S.3
McDonald, N.Q.4
Treisman, R.5
-
10
-
-
34250849566
-
Nuclear actin regulates dynamic subcellular localization and activity of the SRF cofactor MAL
-
10 Vartiainen, M.K., Guettler, S., Larijani, B., Treisman, R., Nuclear actin regulates dynamic subcellular localization and activity of the SRF cofactor MAL. Science 316 (2007), 1749–1752.
-
(2007)
Science
, vol.316
, pp. 1749-1752
-
-
Vartiainen, M.K.1
Guettler, S.2
Larijani, B.3
Treisman, R.4
-
11
-
-
84988632757
-
Nuclear actin modulates cell motility via transcriptional regulation of adhesive and cytoskeletal genes
-
11 Sharili, A.S., Kenny, F.N., Vartiainen, M.K., Connelly, J.T., Nuclear actin modulates cell motility via transcriptional regulation of adhesive and cytoskeletal genes. Sci Rep, 6, 2016.
-
(2016)
Sci Rep
, vol.6
-
-
Sharili, A.S.1
Kenny, F.N.2
Vartiainen, M.K.3
Connelly, J.T.4
-
12
-
-
84895076694
-
Redox modification of nuclear actin by MICAL-2 regulates SRF signaling
-
This paper demonstrates a novel mechanism to regulate actin via an atypical actin-regulatory protein MICAL-2 in the nucleus. This pathway impinges on SRF activity and MICAL-2 is further demonstrated to be a target of a small molecule inhibitor of clinical relevance.
-
12•• Lundquist, M.R., Storaska, A.J., Liu, T.-C., Larsen, S.D., Evans, T., Neubig, R.R., Jaffrey, S.R., Redox modification of nuclear actin by MICAL-2 regulates SRF signaling. Cell 156 (2014), 563–576 This paper demonstrates a novel mechanism to regulate actin via an atypical actin-regulatory protein MICAL-2 in the nucleus. This pathway impinges on SRF activity and MICAL-2 is further demonstrated to be a target of a small molecule inhibitor of clinical relevance.
-
(2014)
Cell
, vol.156
, pp. 563-576
-
-
Lundquist, M.R.1
Storaska, A.J.2
Liu, T.-C.3
Larsen, S.D.4
Evans, T.5
Neubig, R.R.6
Jaffrey, S.R.7
-
13
-
-
84878116428
-
Lamin A/C and emerin regulate MKL1-SRF activity by modulating actin dynamics
-
13 Ho, C.Y., Jaalouk, D.E., Vartiainen, M.K., Lammerding, J., Lamin A/C and emerin regulate MKL1-SRF activity by modulating actin dynamics. Nature 497 (2013), 507–511.
-
(2013)
Nature
, vol.497
, pp. 507-511
-
-
Ho, C.Y.1
Jaalouk, D.E.2
Vartiainen, M.K.3
Lammerding, J.4
-
14
-
-
84935465337
-
Genome-wide RNAi screen for nuclear actin reveals a network of cofilin regulators
-
14 Dopie, J., Rajakylä, E.K., Joensuu, M.S., Huet, G., Ferrantelli, E., Xie, T., Jäälinoja, H., Jokitalo, E., Vartiainen, M.K., Genome-wide RNAi screen for nuclear actin reveals a network of cofilin regulators. J Cell Sci 128 (2015), 2388–2400.
-
(2015)
J Cell Sci
, vol.128
, pp. 2388-2400
-
-
Dopie, J.1
Rajakylä, E.K.2
Joensuu, M.S.3
Huet, G.4
Ferrantelli, E.5
Xie, T.6
Jäälinoja, H.7
Jokitalo, E.8
Vartiainen, M.K.9
-
15
-
-
84982730582
-
Phosphorylation acts positively and negatively to regulate MRTF-A subcellular localisation and activity
-
This study explains the intricate crosstalk between actin-binding and phosphorylation in the regulation of MKL1 activity, and identifies both positive and negative regulatory modes.
-
15• Panayiotou, R., Miralles, F., Pawlowski, R., Diring, J., Flynn, H.R., Skehel, M., Treisman, R., Phosphorylation acts positively and negatively to regulate MRTF-A subcellular localisation and activity. Elife, 5, 2016, e15460 This study explains the intricate crosstalk between actin-binding and phosphorylation in the regulation of MKL1 activity, and identifies both positive and negative regulatory modes.
-
(2016)
Elife
, vol.5
, pp. e15460
-
-
Panayiotou, R.1
Miralles, F.2
Pawlowski, R.3
Diring, J.4
Flynn, H.R.5
Skehel, M.6
Treisman, R.7
-
16
-
-
43249090629
-
The HSA domain binds nuclear actin-related proteins to regulate chromatin-remodeling ATPases
-
16 Szerlong, H., Hinata, K., Viswanathan, R., Erdjument-Bromage, H., Tempst, P., Cairns, B.R., The HSA domain binds nuclear actin-related proteins to regulate chromatin-remodeling ATPases. Nat Struct Mol Biol 15 (2008), 469–476.
-
(2008)
Nat Struct Mol Biol
, vol.15
, pp. 469-476
-
-
Szerlong, H.1
Hinata, K.2
Viswanathan, R.3
Erdjument-Bromage, H.4
Tempst, P.5
Cairns, B.R.6
-
17
-
-
79957907752
-
Structural biochemistry of nuclear actin-related proteins 4 and 8 reveals their interaction with actin
-
17 Fenn, S., Breitsprecher, D., Gerhold, C.B., Witte, G., Faix, J., Hopfner, K.-P., Structural biochemistry of nuclear actin-related proteins 4 and 8 reveals their interaction with actin. EMBO J 30 (2011), 2153–2166.
-
(2011)
EMBO J
, vol.30
, pp. 2153-2166
-
-
Fenn, S.1
Breitsprecher, D.2
Gerhold, C.B.3
Witte, G.4
Faix, J.5
Hopfner, K.-P.6
-
18
-
-
84876166087
-
Evidence for monomeric actin function in INO80 chromatin remodeling
-
18 Kapoor, P., Chen, M., Winkler, D.D., Luger, K., Shen, X., Evidence for monomeric actin function in INO80 chromatin remodeling. Nat Struct Mol Biol 20 (2013), 426–432.
-
(2013)
Nat Struct Mol Biol
, vol.20
, pp. 426-432
-
-
Kapoor, P.1
Chen, M.2
Winkler, D.D.3
Luger, K.4
Shen, X.5
-
19
-
-
84982883592
-
Crystal structure of a nuclear actin ternary complex
-
Structural studies show the peculiar, twisted orientation of actin in complex with Arp4 and the HSA domain of chromatin remodeler Swr1. This structure frees actin from ATP-binding, and can explain how actin operates differently in the nucleus compared to cytoplasm.
-
19• Cao, T., Sun, L., Jiang, Y., Huang, S., Wang, J., Chen, Z., Crystal structure of a nuclear actin ternary complex. Proc Natl Acad Sci U S A 113 (2016), 8985–8990 Structural studies show the peculiar, twisted orientation of actin in complex with Arp4 and the HSA domain of chromatin remodeler Swr1. This structure frees actin from ATP-binding, and can explain how actin operates differently in the nucleus compared to cytoplasm.
-
(2016)
Proc Natl Acad Sci U S A
, vol.113
, pp. 8985-8990
-
-
Cao, T.1
Sun, L.2
Jiang, Y.3
Huang, S.4
Wang, J.5
Chen, Z.6
-
20
-
-
84884228389
-
Structure and subunit topology of the INO80 chromatin remodeler and its nucleosome complex
-
20 Tosi, A., Haas, C., Herzog, F., Gilmozzi, A., Berninghausen, O., Ungewickell, C., Gerhold, C.B., Lakomek, K., Aebersold, R., Beckmann, R., et al. Structure and subunit topology of the INO80 chromatin remodeler and its nucleosome complex. Cell 154 (2013), 1207–1219.
-
(2013)
Cell
, vol.154
, pp. 1207-1219
-
-
Tosi, A.1
Haas, C.2
Herzog, F.3
Gilmozzi, A.4
Berninghausen, O.5
Ungewickell, C.6
Gerhold, C.B.7
Lakomek, K.8
Aebersold, R.9
Beckmann, R.10
-
21
-
-
84976371088
-
A role for nuclear actin in HDAC 1 and 2 regulation
-
21 Serebryannyy, L.A., Cruz, C.M., de Lanerolle, P., A role for nuclear actin in HDAC 1 and 2 regulation. Sci Rep, 2016, 10.1038/srep28460.
-
(2016)
Sci Rep
-
-
Serebryannyy, L.A.1
Cruz, C.M.2
de Lanerolle, P.3
-
22
-
-
10344264971
-
Nuclear actin and myosin I are required for RNA polymerase I transcription
-
22 Philimonenko, V.V., Zhao, J., Iben, S., Dingová, H., Kysela, K., Kahle, M., Zentgraf, H., Hofmann, W.A., de Lanerolle, P., Hozak, P., et al. Nuclear actin and myosin I are required for RNA polymerase I transcription. Nat Cell Biol 6 (2004), 1165–1172.
-
(2004)
Nat Cell Biol
, vol.6
, pp. 1165-1172
-
-
Philimonenko, V.V.1
Zhao, J.2
Iben, S.3
Dingová, H.4
Kysela, K.5
Kahle, M.6
Zentgraf, H.7
Hofmann, W.A.8
de Lanerolle, P.9
Hozak, P.10
-
23
-
-
7944239067
-
Actin is part of pre-initiation complexes and is necessary for transcription by RNA polymerase II
-
23 Hofmann, W.A., Stojiljkovic, L., Fuchsova, B., Vargas, G.M., Mavrommatis, E., Philimonenko, V., Kysela, K., Goodrich, J.A., Lessard, J.L., Hope, T.J., et al. Actin is part of pre-initiation complexes and is necessary for transcription by RNA polymerase II. Nat Cell Biol 6 (2004), 1094–1101.
-
(2004)
Nat Cell Biol
, vol.6
, pp. 1094-1101
-
-
Hofmann, W.A.1
Stojiljkovic, L.2
Fuchsova, B.3
Vargas, G.M.4
Mavrommatis, E.5
Philimonenko, V.6
Kysela, K.7
Goodrich, J.A.8
Lessard, J.L.9
Hope, T.J.10
-
24
-
-
53549100755
-
The histone acetyltransferase PCAF associates with actin and hnRNP U for RNA polymerase II transcription
-
24 Obrdlik, A., Kukalev, A., Louvet, E., Farrants, A.-K.O., Caputo, L., Percipalle, P., The histone acetyltransferase PCAF associates with actin and hnRNP U for RNA polymerase II transcription. Mol Cell Biol 28 (2008), 6342–6357.
-
(2008)
Mol Cell Biol
, vol.28
, pp. 6342-6357
-
-
Obrdlik, A.1
Kukalev, A.2
Louvet, E.3
Farrants, A.-K.O.4
Caputo, L.5
Percipalle, P.6
-
25
-
-
10644294832
-
A role for beta-actin in RNA polymerase III transcription
-
25 Hu, P., Wu, S., Hernandez, N., A role for beta-actin in RNA polymerase III transcription. Genes Dev 18 (2004), 3010–3015.
-
(2004)
Genes Dev
, vol.18
, pp. 3010-3015
-
-
Hu, P.1
Wu, S.2
Hernandez, N.3
-
26
-
-
79955396454
-
G-actin participates in RNA polymerase II-dependent transcription elongation by recruiting positive transcription elongation factor b (P-TEFb)
-
26 Qi, T., Tang, W., Wang, L., Zhai, L., Guo, L., Zeng, X., G-actin participates in RNA polymerase II-dependent transcription elongation by recruiting positive transcription elongation factor b (P-TEFb). J Biol Chem 286 (2011), 15171–15181.
-
(2011)
J Biol Chem
, vol.286
, pp. 15171-15181
-
-
Qi, T.1
Tang, W.2
Wang, L.3
Zhai, L.4
Guo, L.5
Zeng, X.6
-
27
-
-
78751633931
-
Depletion of nuclear actin is a key mediator of quiescence in epithelial cells
-
27 Spencer, V.A., Costes, S., Inman, J.L., Xu, R., Chen, J., Hendzel, M.J., Bissell, M.J., Depletion of nuclear actin is a key mediator of quiescence in epithelial cells. J Cell Sci 124 (2011), 123–132.
-
(2011)
J Cell Sci
, vol.124
, pp. 123-132
-
-
Spencer, V.A.1
Costes, S.2
Inman, J.L.3
Xu, R.4
Chen, J.5
Hendzel, M.J.6
Bissell, M.J.7
-
28
-
-
84978174328
-
Mechanical regulation of transcription controls Polycomb-mediated gene silencing during lineage commitment
-
This study links nuclear actin levels to stem cell lineage commitment. The study shows for the first time that mechanical regulation impact nuclear organization via regulation of nuclear actin levels. Mechanistically, mechanical regulation of emerin localization controls nuclear import competent actin levels, and consequently transcription.
-
28•• Le, H.Q., Ghatak, S., Yeung, C.-Y.C., Tellkamp, F., Günschmann, C., Dieterich, C., Yeroslaviz, A., Habermann, B., Pombo, A., Niessen, C.M., et al. Mechanical regulation of transcription controls Polycomb-mediated gene silencing during lineage commitment. Nat Cell Biol 18 (2016), 864–875 This study links nuclear actin levels to stem cell lineage commitment. The study shows for the first time that mechanical regulation impact nuclear organization via regulation of nuclear actin levels. Mechanistically, mechanical regulation of emerin localization controls nuclear import competent actin levels, and consequently transcription.
-
(2016)
Nat Cell Biol
, vol.18
, pp. 864-875
-
-
Le, H.Q.1
Ghatak, S.2
Yeung, C.-Y.C.3
Tellkamp, F.4
Günschmann, C.5
Dieterich, C.6
Yeroslaviz, A.7
Habermann, B.8
Pombo, A.9
Niessen, C.M.10
-
29
-
-
84933038827
-
Nuclear myosin 1 contributes to a chromatin landscape compatible with RNA polymerase II transcription activation
-
29 Almuzzaini, B., Sarshad, A.A., Farrants, A.-K.O., Percipalle, P., Nuclear myosin 1 contributes to a chromatin landscape compatible with RNA polymerase II transcription activation. BMC Biol, 13, 2015, 35.
-
(2015)
BMC Biol
, vol.13
, pp. 35
-
-
Almuzzaini, B.1
Sarshad, A.A.2
Farrants, A.-K.O.3
Percipalle, P.4
-
30
-
-
79952637148
-
The F-actin severing protein cofilin-1 is required for RNA polymerase II transcription elongation
-
30 Obrdlik, A., Percipalle, P., The F-actin severing protein cofilin-1 is required for RNA polymerase II transcription elongation. Nucleus 2 (2014), 72–79.
-
(2014)
Nucleus
, vol.2
, pp. 72-79
-
-
Obrdlik, A.1
Percipalle, P.2
-
31
-
-
34147105329
-
A novel role of the actin-nucleating Arp2/3 complex in the regulation of RNA polymerase II-dependent transcription
-
31 Yoo, Y., Wu, X., Guan, J.-L., A novel role of the actin-nucleating Arp2/3 complex in the regulation of RNA polymerase II-dependent transcription. J Biol Chem 282 (2007), 7616–7623.
-
(2007)
J Biol Chem
, vol.282
, pp. 7616-7623
-
-
Yoo, Y.1
Wu, X.2
Guan, J.-L.3
-
32
-
-
33745762947
-
Regulation of RNA-polymerase-II-dependent transcription by N-WASP and its nuclear-binding partners
-
32 Wu, X., Yoo, Y., Okuhama, N.N., Tucker, P.W., Liu, G., Guan, J.-L., Regulation of RNA-polymerase-II-dependent transcription by N-WASP and its nuclear-binding partners. Nat Cell Biol 8 (2006), 756–763.
-
(2006)
Nat Cell Biol
, vol.8
, pp. 756-763
-
-
Wu, X.1
Yoo, Y.2
Okuhama, N.N.3
Tucker, P.W.4
Liu, G.5
Guan, J.-L.6
-
33
-
-
85052276775
-
Co-transcriptional nuclear actin dynamics
-
33 Percipalle, P., Co-transcriptional nuclear actin dynamics. Nucleus 4 (2013), 43–52.
-
(2013)
Nucleus
, vol.4
, pp. 43-52
-
-
Percipalle, P.1
-
34
-
-
84988447968
-
Persistent nuclear actin filaments inhibit transcription by RNA polymerase II
-
By inducing stable actin filaments in the nucleus, this study sheds light on the functional form of actin during transcription. Their results demonstrate a role for dynamic actin in transcription by RNA polymerase II, and further studies enforce the role of actin monomers in this context.
-
34• Serebryannyy, L.A., Parilla, M., Annibale, P., Cruz, C.M., Laster, K., Gratton, E., Kudryashov, D., Kosak, S.T., Gottardi, C.J., de Lanerolle, P., Persistent nuclear actin filaments inhibit transcription by RNA polymerase II. J Cell Sci, 2016, 10.1242/jcs.195867 By inducing stable actin filaments in the nucleus, this study sheds light on the functional form of actin during transcription. Their results demonstrate a role for dynamic actin in transcription by RNA polymerase II, and further studies enforce the role of actin monomers in this context.
-
(2016)
J Cell Sci
-
-
Serebryannyy, L.A.1
Parilla, M.2
Annibale, P.3
Cruz, C.M.4
Laster, K.5
Gratton, E.6
Kudryashov, D.7
Kosak, S.T.8
Gottardi, C.J.9
de Lanerolle, P.10
-
35
-
-
33644747345
-
A selective block of nuclear actin export stabilizes the giant nuclei of Xenopus oocytes
-
35 Bohnsack, M.T., Stüven, T., Kuhn, C., Cordes, V.C., Görlich, D., A selective block of nuclear actin export stabilizes the giant nuclei of Xenopus oocytes. Nat Cell Biol 8 (2006), 257–263.
-
(2006)
Nat Cell Biol
, vol.8
, pp. 257-263
-
-
Bohnsack, M.T.1
Stüven, T.2
Kuhn, C.3
Cordes, V.C.4
Görlich, D.5
-
36
-
-
84885179258
-
A nuclear F-actin scaffold stabilizes ribonucleoprotein droplets against gravity in large cells
-
36 Feric, M., Brangwynne, C.P., A nuclear F-actin scaffold stabilizes ribonucleoprotein droplets against gravity in large cells. Nat Cell Biol 15 (2013), 1253–1259.
-
(2013)
Nat Cell Biol
, vol.15
, pp. 1253-1259
-
-
Feric, M.1
Brangwynne, C.P.2
-
37
-
-
77349090693
-
Rapid chromosome territory relocation by nuclear motor activity in response to serum removal in primary human fibroblasts
-
37 Mehta, I.S., Amira, M., Harvey, A.J., Bridger, J.M., Rapid chromosome territory relocation by nuclear motor activity in response to serum removal in primary human fibroblasts. Genome Biol, 11, 2010, R5.
-
(2010)
Genome Biol
, vol.11
, pp. R5
-
-
Mehta, I.S.1
Amira, M.2
Harvey, A.J.3
Bridger, J.M.4
-
38
-
-
33646021963
-
Long-range directional movement of an interphase chromosome site
-
38 Chuang, C.-H., Carpenter, A.E., Fuchsova, B., Johnson, T., de Lanerolle, P., Belmont, A.S., Long-range directional movement of an interphase chromosome site. Curr Biol 16 (2006), 825–831.
-
(2006)
Curr Biol
, vol.16
, pp. 825-831
-
-
Chuang, C.-H.1
Carpenter, A.E.2
Fuchsova, B.3
Johnson, T.4
de Lanerolle, P.5
Belmont, A.S.6
-
39
-
-
37249038708
-
Actin-dependent intranuclear repositioning of an active gene locus in vivo
-
39 Dundr, M., Ospina, J.K., Sung, M.-H., John, S., Upender, M., Ried, T., Hager, G.L., Matera, A.G., Actin-dependent intranuclear repositioning of an active gene locus in vivo. J Cell Biol 179 (2007), 1095–1103.
-
(2007)
J Cell Biol
, vol.179
, pp. 1095-1103
-
-
Dundr, M.1
Ospina, J.K.2
Sung, M.-H.3
John, S.4
Upender, M.5
Ried, T.6
Hager, G.L.7
Matera, A.G.8
-
40
-
-
84901194830
-
HSP70 transgene directed motion to nuclear speckles facilitates heat shock activation
-
By using sophisticated imaging methods, this paper demonstrates directed, actin-dependent movement of a gene locus upon transcription activation. For the first time, this study demonstrates directly the link between the movement and gene activation.
-
40•• Khanna, N., Hu, Y., Belmont, A.S., HSP70 transgene directed motion to nuclear speckles facilitates heat shock activation. Curr Biol 24 (2014), 1138–1144 By using sophisticated imaging methods, this paper demonstrates directed, actin-dependent movement of a gene locus upon transcription activation. For the first time, this study demonstrates directly the link between the movement and gene activation.
-
(2014)
Curr Biol
, vol.24
, pp. 1138-1144
-
-
Khanna, N.1
Hu, Y.2
Belmont, A.S.3
-
41
-
-
84879105224
-
Proximity to PML nuclear bodies regulates HIV-1 latency in CD4+ T cells
-
41 Lusic, M., Marini, B., Ali, H., Lucic, B., Luzzati, R., Giacca, M., Proximity to PML nuclear bodies regulates HIV-1 latency in CD4+ T cells. Cell Host Microbe 13 (2013), 665–677.
-
(2013)
Cell Host Microbe
, vol.13
, pp. 665-677
-
-
Lusic, M.1
Marini, B.2
Ali, H.3
Lucic, B.4
Luzzati, R.5
Giacca, M.6
-
42
-
-
84971500228
-
Diaphanous formin mDia2 regulates CENP-A levels at centromeres
-
This study describes a novel mechanism to maintain centromere identity by demonstrating that the formin mDia2 operates downstream of MgcRacGAP to control CENP-A loading to centromers via its chaperone HJURP. These findings suggest a role for nuclear actin polymerization in the context of regulation nucleosome composition at centromeres.
-
42• Liu, C., Mao, Y., Diaphanous formin mDia2 regulates CENP-A levels at centromeres. J Cell Biol 213 (2016), 415–424 This study describes a novel mechanism to maintain centromere identity by demonstrating that the formin mDia2 operates downstream of MgcRacGAP to control CENP-A loading to centromers via its chaperone HJURP. These findings suggest a role for nuclear actin polymerization in the context of regulation nucleosome composition at centromeres.
-
(2016)
J Cell Biol
, vol.213
, pp. 415-424
-
-
Liu, C.1
Mao, Y.2
|