NMR structure of the calponin homology domain of human IQGAP1 and its implications for the actin recognition mode

Umemoto, Ryo; Nishida, N.; Ogino, Shuichi; Shimada, Ichio

doi:10.1007/s10858-010-9434-8

Cited by 14 publications

(18 citation statements)

References 19 publications

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“…To determine if IQGAP1 mitotic function is regulated by phosphorylation, we performed quantitative mass spectrometry to identify all phosphorylation sites on human IQGAP1 that are upregulated during mitosis. Immunoblotting and mass spectrometry identified similar amounts of IQGAP1 and its binding partners actin and myosin, [62][63][64] in all cell cycle phases (Fig. 5A, lower panel).…”

Section: Iqgap1 Regulates the Timing Of Npc Reassemblymentioning

confidence: 90%

IQGAP1 is associated with nuclear envelope reformation and completion of abscission

et al. 2015

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The final stage of mitosis is cytokinesis, which results in 2 independent daughter cells. Cytokinesis has 2 phases: membrane ingression followed by membrane abscission. IQGAP1 is a scaffold protein that interacts with proteins implicated in mitosis, including F-actin, myosin and CaM. IQGAP1 in yeast recruits actin and myosin II filaments to the contractile ring for membrane ingression. In contrast, we show that mammalian IQGAP1 is not required for ingression, but coordinates nuclear pore complex (NPC) reassembly and completion of abscission. Depletion of IQGAP1 disrupts Nup98 and mAb414 nuclear envelope localization and delays abscission timing. IQGAP1 phosphorylation increases 15-fold upon mitotic entry at S86, S330 and T1434, with the latter site being targeted by CDK2/Cyclin A and CDK1/Cyclin A/ B in vitro. Expressing the phospho-deficient mutant IQGAP1-S330A impairs NPC reassembly in cells undergoing abscission. Thus, mammalian IQGAP1 functions later in mitosis than its yeast counterpart to regulate nuclear pore assembly in a S330 phosphorylation-dependent manner during the abscission phase of cytokinesis.

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Section: Iqgap1 Regulates the Timing Of Npc Reassemblymentioning

confidence: 90%

IQGAP1 is associated with nuclear envelope reformation and completion of abscission

et al. 2015

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“…The association of F-actin with the CHD is a function conserved with several other actin-binding proteins. However, while most actin-binding proteins bind F-actin via tandem CHDs, IQGAP1 forms a high affinity interaction with F-actin through a single CHD [99, 100]. Additionally, the IQGAP1 CHD associates with calmodulin and Ca 2+ [12].…”

Section: Iqgaps Regulate Cellular Functionsmentioning

confidence: 99%

IQGAPs choreograph cellular signaling from the membrane to the nucleus

Smith

Hedman

Sacks

2015

Trends in Cell Biology

140

154

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Since its discovery in 1994, cellular functions for the scaffold protein IQGAP1 have expanded immensely. Over 100 unique IQGAP1 interacting proteins have been identified, implicating IQGAP1 as a critical integrator of cellular signaling pathways. Initial research established functions for IQGAP1 in cell-cell adhesion, cell migration, and cell signaling. Recent studies have revealed additional IQGAP1 binding partners, expanding the biological roles of IQGAP1. These include crosstalk between signaling cascades, regulation of nuclear function, and Wnt pathway potentiation. Investigation of the IQGAP2 and IQGAP3 homologues demonstrate unique functions, some of which differ from those of IQGAP1. Summarized here are recent observations that enhance our understanding of IQGAP proteins in integrating diverse signaling pathways.

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“…Conserved proline residues are outlined in black. Shaded regions indicate alpha-helices previously determined for the CH domain of IQGAP1 (Umemoto et al , 2010) and predicted for Iqg1p using PSIPRED analysis software (UCL Bioinformatics). B) Diagram of Iqg1p-mediated functions involved in cytoskeletal remodeling in yeast mirrors what has been shown for C) IQGAP1 in mammalian cells such as lymphocytes.…”

Section: Figurementioning

confidence: 99%

IQGAP1: Insights into the function of a molecular puppeteer

Abel

Schuldt

Rajasekaran

et al. 2015

Molecular Immunology

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The intracellular spatiotemporal organization of signaling events is critical for normal cellular function. In response to environmental stimuli, cells utilize highly organized signaling pathways that are subject to multiple layers of regulation. However, the molecular mechanisms that coordinate these complex processes remain an enigma. Scaffolding proteins (scaffolins) have emerged as critical regulators of signaling pathways, many of which have well-described functions in immune cells. IQGAP1, a highly conserved cytoplasmic scaffold protein, is able to curb, compartmentalize, and coordinate multiple signaling pathways in a variety of cell types. IQGAP1 plays a central role in cell-cell interaction, cell adherence, and movement via actin/tubulin-based cytoskeletal reorganization. Evidence also implicates IQGAP1 as an essential regulator of the MAPK and Wnt/β-catenin signaling pathways. Here, we summarize the recent advances on the cellular and molecular biology of IQGAP1. We also describe how this pleiotropic scaffolin acts as a true molecular puppeteer, and highlight the significance of future research regarding the role of IQGAP1 in immune cells.

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NMR structure of the calponin homology domain of human IQGAP1 and its implications for the actin recognition mode

Cited by 14 publications

References 19 publications

IQGAP1 is associated with nuclear envelope reformation and completion of abscission

IQGAP1 is associated with nuclear envelope reformation and completion of abscission

IQGAPs choreograph cellular signaling from the membrane to the nucleus

IQGAP1: Insights into the function of a molecular puppeteer

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