Results 51 to 60 of about 1,114,768 (261)

Nucleocytoplasmic Shuttling of Cytoskeletal Proteins: Molecular Mechanism and Biological Significance

open access: yesInternational Journal of Cell Biology, 2012
Various nuclear functional complexes contain cytoskeletal proteins as regulatory subunits; for example, nuclear actin participates in transcriptional complexes, and actin-related proteins are integral to chromatin remodeling complexes.
Masahiro Kumeta   +3 more
doaj   +1 more source

Valosin‐containing protein counteracts ATP‐driven dissolution of FUS condensates through its ATPase activity in vitro

open access: yesFEBS Letters, EarlyView.
Biomolecular condensates formed by fused in sarcoma (FUS) are dissolved by high ATP concentrations yet persist in cells. Using a reconstituted system, we demonstrate that valosin‐containing protein (VCP), an AAA+ ATPase, counteracts ATP‐driven dissolution of FUS condensates through its D2 ATPase activity.
Hitomi Kimura   +2 more
wiley   +1 more source

Nuclear Polyadenylate-Binding Protein [PDF]

open access: yesMolecular and Cellular Biology, 1985
Polyadenylate-binding activity can be detected in eluates from sodium dodecyl sulfate gels by a nitrocellulose filter-binding assay. Nuclear extracts from rat liver show a single peak of binding activity at 50 to 55 kilodaltons; cytoplasmic extracts show a single peak at 70 to 80 kilodaltons, corresponding to a 75-kilodalton protein previously ...
A B, Sachs, R D, Kornberg
openaire   +2 more sources

Hyperosmotic stress induces PARP1‐mediated HPF1‐dependent mono(ADP‐ribosyl)ation

open access: yesFEBS Letters, EarlyView.
Sorbitol‐induced hyperosmotic stress rapidly induces reversible mono(ADP‐ribosyl)ation (MARylation) on PARP1 without the signs of genotoxic signaling. We show that PARP1 autoMARylation is HPF1 dependent and forms hydroxylamine‐resistant O‐glycosidic linkages.
Anna Georgina Kopasz   +11 more
wiley   +1 more source

Transcriptional repression and cell death induced by nuclear aggregates of non-polyglutamine protein

open access: yesNeurobiology of Disease, 2005
Nuclear aggregates of polyglutamine (polyQ)-expanded proteins are associated with a number of neurodegenerative diseases including Huntington's disease (HD) and spinocerebellar ataxias (SCAs).
Lianwu Fu, Ya-sheng Gao, Elizabeth Sztul
doaj   +1 more source

Types of nuclear localization signals and mechanisms of protein import into the nucleus

open access: yesCell Communication and Signaling, 2021
Nuclear localization signals (NLS) are generally short peptides that act as a signal fragment that mediates the transport of proteins from the cytoplasm into the nucleus.
Juane Lu   +6 more
doaj   +1 more source

An isoform of 14‐3‐3 protein regulates transbilayer lipid movement at the plasma membrane

open access: yesFEBS Letters, EarlyView.
Loss of 14‐3‐3ζ in CHO cells confers resistance to exogenous phosphatidylserine (PS) and impairs endocytosis‐independent inward flip‐flop of fluorescent PS at the plasma membrane. RNAi‐mediated knockdown reproduces this defect, while no additive effect is seen in ATP11C‐deficient cells.
Akiko Yamaji‐Hasegawa   +3 more
wiley   +1 more source

Organizing the interface—Plasma membrane architecture and receptor dynamics in virus‐cell interactions

open access: yesFEBS Letters, EarlyView.
Plasma membranes contain dynamic nanoscale domains that organize lipids and receptors. Because viruses operate at similar scales, this architecture shapes early infection steps, including attachment, receptor engagement, and entry. Using influenza A virus and HIV‐1 as examples, we highlight how receptor nanoclusters, multivalent glycan interactions ...
Jan Schlegel, Christian Sieben
wiley   +1 more source

Biophysical approaches for studying viral entry

open access: yesFEBS Letters, EarlyView.
Viruses infect all living organisms and have been responsible for major epidemics and pandemics. Their ongoing evolutionary battle with host defenses creates a constant need for improved tools to study viral behavior. Advancing methods to probe viral attachment, fusion, and genome release deepen our understanding of how infections begin and support the
Inbar Yosibash, Raya Sorkin
wiley   +1 more source

Septin 9 PB domains coordinate centrosome positioning and microtubule acetylation to control epithelial polarity

open access: yesFEBS Letters, EarlyView.
Septin 9 polybasic domains couple phosphoinositide‐rich membrane binding to centrosome positioning, Golgi organization, and microtubule acetylation to control epithelial polarity. Their loss disrupts this axis, causing centrosome mispositioning, Golgi fragmentation, reduced microtubule acetylation, and polarity inversion via upregulation of the ...
Ting ting Cai   +4 more
wiley   +1 more source

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