Results 131 to 140 of about 21,607 (213)

Novel localization of formin mDia2: importin β-mediated delivery to and retention at the cytoplasmic side of the nuclear envelope

Biology Open, 2015
The formin family proteins are important regulators of actin polymerization that are involved in many cellular processes. However, little is known about their specific cellular localizations.
Xiaowei Shao, Keiko Kawauchi, G. V. Shivashankar, Alexander D. Bershadsky   +3 more
doaj   +1 more source

The adapter importin‐α provides flexible control of nuclear import at the expense of efficiency

Molecular Systems Biology, 2007
Although there exists a large family of nuclear transport receptors (Karyopherins), the majority of known import cargoes use an adapter protein, Importin‐α (Impα), which links the cargo to a karyopherin, Importin‐β (Impβ). The reason for the existence of
Greg Riddick, Ian G Macara
doaj   +1 more source

Probing formation of cargo/importin-α transport complexes in plant cells using a pathogen effector [PDF]

, 2015
Importin-αs are essential adapter proteins that recruit cytoplasmic proteins destined for active nuclear import to the nuclear transport machinery. Cargo proteins interact with the importin-α armadillo repeat domain via nuclear localization sequences ...
Wirthmueller, Lennart, Roth, Charlotte, Jones, Jonathan D. G., Fabro, Georgina, Jonathan D. G. Jones, Banfield, Mark J., Georgina Fabro, Shuta Asai, Wiermer, Marcel, Caillaud, Marie-Cécile, Charlotte Roth, Jones, Alexandra M., Marie‐Cécile Caillaud, Marcel Wiermer, Lennart Wirthmueller, Jones, Alexandra M. E., Asai, Shuta, Alexandra M. E. Jones, Rallapalli, Ghanasyam, Ghanasyam Rallapalli, Sklenar, Jan, Mark J. Banfield, Jan Sklenar   +22 more
core   +1 more source

Nup98 FG domains from diverse species spontaneously phase-separate into particles with nuclear pore-like permselectivity

eLife, 2015
Nuclear pore complexes (NPCs) conduct massive transport mediated by shuttling nuclear transport receptors (NTRs), while keeping nuclear and cytoplasmic contents separated.
Hermann Broder Schmidt, Dirk Görlich
doaj   +1 more source

Exploring the role of mononuclear phagocytes in the epididymis

Asian Journal of Andrology, 2015
The onslaught of foreign antigens carried by spermatozoa into the epididymis, an organ that has not demonstrated immune privilege, a decade or more after the establishment of central immune tolerance presents a unique biological challenge.
Nicolas Da Silva, Tegan B Smith
doaj   +1 more source

Importin subunit beta‐1 mediates ERK5 nuclear translocation, and its inhibition synergizes with ERK5 kinase inhibitors in reducing cancer cell proliferation

Molecular Oncology
The mitogen‐activated protein kinase (MAPK) extracellular signal‐regulated kinase 5 (ERK5) is emerging as a promising target in cancer. Indeed, alterations of the MEK5/ERK5 pathway are present in many types of cancer, including melanoma.
Zoe Lombardi, Lucia Gardini, Anatolii V. Kashchuk, Alessio Menconi, Matteo Lulli, Ignazia Tusa, Alessandro Tubita, Luisa Maresca, Barbara Stecca, Marco Capitanio, Elisabetta Rovida   +10 more
doaj   +1 more source

Ligands binding diffusively to protein target act as inhibitors of protein-protein interactions.

PLoS Computational Biology
Nuclear localization signal (NLS) sequence from capsid protein of Venezuelan equine encephalitis virus (VEEV) binds to importin-α transport protein and clogs nuclear import. Prevention of viral NLS binding to importin-α may represent a viable therapeutic
William Jeffries, Bryan M Delfing, Xavier E Laracuente, Xingyu Luo, Audrey Olson, Kenneth W Foreman, Kyung Hyeon Lee, Greg Petruncio, Vito De Benedictis, Mikell Paige, Kylene Kehn-Hall, Christopher Lockhart, Dmitri K Klimov   +12 more
doaj   +1 more source

Evidence for distinct substrate specificities of importin α family members in nuclear protein import. [PDF]

, 1999
Importin α plays a pivotal role in the classical nuclear protein import pathway. Importin α shuttles between nucleus and cytoplasm, binds nuclear localization signal-bearing proteins, and functions as an adapter to access the importin β-dependent import ...
Prehn, S., Koehler, M., Hartmann, E., Bischoff, F., Köhler, M., Görlich, D., Goerlich, D., Haller, H., Speck, C., Bischoff, F.R., Christiansen, M.   +10 more
core  

Nuclear localization signal and protein context both mediate importin α specificity of nuclear import substrates

, 2006
The 'classical' nuclear protein import pathway depends on importin alpha and importin beta. Importin alpha binds nuclear localization signal (NLS)-bearing proteins and functions as an adapter to access the importin beta dependent import pathway.
Sommer, T., Koehler, M., Hartmann, E., Quensel, C., Friedrich, B.   +4 more
core   +1 more source

Importin alpha associates with membranes and participates in nuclear envelope assembly in vitro [PDF]

Importin alpha is well known as an adaptor that functions with Importin beta in the nuclear import of proteins containing specific nuclear localization signals (NLSs). We show here that either an excess or a lack of Importin alpha blocks nuclear envelope
Köcher, Thomas, Wilm, Matthias, Hachet, Virginie, Mattaj, Iain W.   +3 more
core   +1 more source