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Regulation of transcription by HIPPI and its molecular partner HIP1

ABSTRACT: Regulation of transcription by HIPPI and its molecular partner HIP1

PROVIDER: PRJNA135327 | ENA |

REPOSITORIES: ENA

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Regulation of transcription by HIPPI and its molecular partner HIP1

Project description:This SuperSeries is composed of the following subset Series: GSE26115: Regulation of transcription by HIP1 protein interactor (HIPPI) in HeLa cells GSE26116: Role of HIP1 in HIPPI mediated transcription regulation in HeLa cells Refer to individual Series

2011-09-20 | E-GEOD-26117 | biostudies-arrayexpress

Role of HIP1 in HIPPI mediated transcription regulation in HeLa cells

2011-09-21 | GSE26116 | GEO

Role of HIP1 in HIPPI mediated transcription regulation in HeLa cells

Project description:Nuclear entry of transcription factor HIPPI is mediated by its interacting partner Huntingtin Interacting Protein 1 (HIP1), a nuclear localization signal containing nucleo-cytoplasmic shuttling protein. In oredr to investigate the role of HIP1 in HIPPI mediated transcriptional regulation in cell, here we performed microarray experiments using stable HIP1 knocked down HeLa cells (Hip1Si) exogenously expressing Green fluorescent protein tagged HIPPI. Total RNA extracted from HIP1 knocked down HeLa cells (Hip1Si) transfected with empty GFP vector served as control and Total RNA extracted from Hip1Si cells transfected with GFP-Hippi construct served as test. Biological replicates: 4

2011-09-20 | E-GEOD-26116 | biostudies-arrayexpress

Auxin and ETT-partner complexes

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Regulation of transcription by HIPPI and its molecular partner HIP1

Project description:This SuperSeries is composed of the SubSeries listed below.

2011-09-21 | GSE26117 | GEO

Molecular and Cellular Mechanisms of Teneurin Signaling in Synaptic Partner Matching

Project description:In the developing brain, axons exhibit remarkable precision in selecting synaptic partners among many non-partner cells. Teneurins are evolutionarily conserved transmembrane proteins that instruct synaptic partner matching via matched expression and homophilic attraction between synaptic partners. Little is known how intracellular signaling pathways execute this and diverse other functions triggered by extracellular interactions of teneurins. Here, we use in situ proximity labeling to identify Ten-ms intracellular interactome in the Drosophila brain. Genetic interaction using quantitative partner matching assays in both olfactory receptor neurons (ORNs) and projection neurons (PNs) suggest a common pathway Ten-m binds to and negatively regulates a RhoGAP, thus activating the Rac1 small GTPases to promote synaptic partner matching. Developmental analyses with single-axon resolution further reveal that ORN axons initially extend exuberant branches along their trajectory, and those that contact partner PN dendrites are selectively stabilized, accompanied by an increase of local F-actin accumulation.

2024-02-05 | MSV000094010 | MassIVE

Redistribution of PU.1 partner transcription factor RUNX1 binding secures cell survival during leukemogenesis

Project description:Redistribution of PU.1 partner transcription factor RUNX1 binding secures cell survival during leukemogenesis

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Transcription regulation of caspase-1 by R393 of HIPPI and its molecular partner HIP-1.

Project description:Earlier we have shown that exogenous expression of HIPPI, a molecular partner of Huntingtin interacting protein HIP-1, induces apoptosis and increases expression of caspases-1, -8 and -10 in HeLa and Neuro2A cells. The C-terminal pseudo death effector domain of HIPPI (pDED-HIPPI) specifically interacts with the putative promoter sequences of these genes. In the present manuscript, we predict from structural modeling of pDED-HIPPI that R393 of HIPPI is important for such interaction. R393E mutation in pDED-HIPPI decreases the interaction with the putative promoter of caspase-1 in cells. Expression of caspase-1 is decreased in cells expressing mutant pDED-HIPPI in comparison to that observed in cells expressing wild type pDED-HIPPI. Using HIP-1 knocked down cells as well as over expressing HIP-1 with mutation at its nuclear localization signal and other deletion mutations, we demonstrate that translocation of HIPPI to the nucleus is mediated by HIP-1 for the increased expression of caspase-1. HIPPI-HIP-1 heterodimer is detected in cytoplasm as well as in the nucleus and is associated with transcription complex in cells. Taking together, we are able to show the importance of R393 of HIPPI and the role of HIPPI-HIP-1 heterodimer in the transcription regulation of caspase-1.

| S-EPMC2817453 | biostudies-literature

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