Publications by authors named "ShuaiYu Liu"

Article Synopsis
  • Dynamic disassembly and reconstruction of the nuclear lamina are crucial for cell division, with CDK1 phosphorylation playing a key role in this process.
  • Mass spectrometry identified specific phosphorylation sites on Lamin A/C during mitosis, with mutations altering phosphorylation status affecting lamina structure and function.
  • Disruption of Lamin A phosphorylation led to nuclear abnormalities, highlighting its importance for nuclear envelope dynamics and maintaining genomic stability during the cell cycle.
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Article Synopsis
  • FOXA1 is a key transcription factor that supports gene expression and maintains cellular identity during development by acting as a mitotic bookmarking factor.
  • During mitosis, FOXA1 primarily dissociates from specific DNA sites but is regulated by Aurora B kinase, which phosphorylates FOXA1 at Serine 221 (S221) to influence its binding behavior.
  • The phosphorylation of S221 affects FOXA1’s ability to bind specific DNA, and disrupting this process can hinder gene reactivation and cell growth, highlighting the importance of reversible phosphorylation for mitotic regulation.
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Although the dynamic instability of microtubules (MTs) is fundamental to many cellular functions, quiescent MTs with unattached free distal ends are commonly present and play important roles in various events to power cellular dynamics. However, how these free MT tips are stabilized remains poorly understood. Here, we report that centrosome and spindle pole protein 1 (CSPP1) caps and stabilizes both plus and minus ends of static MTs.

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The enrichment of histone H3 variant CENP-A is the epigenetic mark of centromere and initiates the assembly of the kinetochore at centromere. The kinetochore is a multi-subunit complex that ensures accurate attachment of microtubule centromere and faithful segregation of sister chromatids during mitosis. As a subunit of kinetochore, CENP-I localization at centromere also depends on CENP-A.

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In eukaryotes, end-binding (EB) proteins serve as a hub for orchestrating microtubule dynamics and are essential for cellular dynamics and organelle movements. EB proteins modulate structural transitions at growing microtubule ends by recognizing and promoting an intermediate state generated during GTP hydrolysis. However, the molecular mechanisms and physiochemical properties of the EB1 interaction network remain elusive.

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As an extracellular matrix protein, secreted protein acidic and rich in cysteine (SPARC)-like 1 (SPARCL1) is involved in various cell functions. It was previously implicated in bovine skeletal muscle-derived satellite cell (MDSC) differentiation; however, the underlying mechanism remains unknown. In this study, immunoprecipitation and mass spectrometry revealed that integrin β1 (ITGB1) combines with SPARCL1.

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The extracellular matrix (ECM) is known to regulate tissue development and cell morphology, movement, and differentiation. SPARCL1 is an ECM protein, but its role in mouse cell differentiation has not been widely investigated. The results of western blotting and immunofluorescence showed that SPARCL1 is associated with the repair of muscle damage in mice and that SPARCL1 binds to bone morphogenetic protein 7 (BMP7) by regulating BMP/transforming growth factor (TGF)-β cell signaling.

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The current work investigates the thermoresponsive in situ chiral to nonchiral ordering transformation of a rodlike virus in the naturally assembled state-the chiral nematic liquid crystal (CLC) phase. We take this as an elegant example of reconfigurable self-assembly, through which it is possible to realize in situ transformation from one assembled state to another without disrupting the preformed assembly in general or going through a secondary assembling procedure of the disassembled building blocks. The detailed investigation presented here reveals many unique characteristics of the thermoresponsive 3D chiral ordering of rodlike viruses induced by heat stress.

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The rodlike M13 viruses with chemically decorated phenylboronic acid moieties form pH responsive chiral nematic liquid crystal (LC) phases. Binding with biologically important diols results in LC phases with microstructures that closely correlate with the molecular structure of the diols and can be conveniently discerned by visual cues.

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