Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

DAKAP1 signaling complexes coordinate local synthesis at the mitochondrial surface

ABSTRACT: dAKAP1 signaling complexes coordinate local synthesis at the mitochondrial surface

PROVIDER: PRJNA575262 | ENA |

REPOSITORIES: ENA

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	SRR10212874_1.fastq.gz	Fastqsanger.gz
	SRR10212874_2.fastq.gz	Fastqsanger.gz
	SRR10212875_1.fastq.gz	Fastqsanger.gz
	SRR10212875_2.fastq.gz	Fastqsanger.gz
	SRR10212876_1.fastq.gz	Fastqsanger.gz

Items per page:

1 - 5 of 26

Similar Datasets

dAKAP1 signaling complexes coordinate local synthesis at the mitochondrial surface

Project description:We find that the KH domain of dAKAP1 binds mRNAs encoding proteins required for mitochondrial metabolism

2020-07-10 | GSE138277 | GEO

A-kinase-anchoring protein 1 (dAKAP1)-based signaling complexes coordinate local protein synthesis at the mitochondrial surface.

Project description:Compartmentalization of macromolecules is a ubiquitous molecular mechanism that drives numerous cellular functions. The appropriate organization of enzymes in space and time enables the precise transmission and integration of intracellular signals. Molecular scaffolds constrain signaling enzymes to influence the regional modulation of these physiological processes. Mitochondrial targeting of protein kinases and protein phosphatases provides a means to locally control the phosphorylation status and action of proteins on the surface of this organelle. Dual-specificity protein kinase A anchoring protein 1 (dAKAP1) is a multivalent binding protein that targets protein kinase A (PKA), RNAs, and other signaling enzymes to the outer mitochondrial membrane. Many AKAPs recruit a diverse set of binding partners that coordinate a broad range of cellular processes. Here, results of MS and biochemical analyses reveal that dAKAP1 anchors additional components, including the ribonucleoprotein granule components La-related protein 4 (LARP4) and polyadenylate-binding protein 1 (PABPC1). Local translation of mRNAs at organelles is a means to spatially control the synthesis of proteins. RNA-Seq data demonstrate that dAKAP1 binds mRNAs encoding proteins required for mitochondrial metabolism, including succinate dehydrogenase. Functional studies suggest that the loss of dAKAP1-RNA interactions reduces mitochondrial electron transport chain activity. Hence, dAKAP1 plays a previously unappreciated role as a molecular interface between second messenger signaling and local protein synthesis machinery.

| S-EPMC7397098 | biostudies-literature

Cortical wiring by synapse type-specific control of local protein synthesis

Project description:Neurons use local protein synthesis to support their morphological complexity, which requires independent control across multiple subcellular compartments up to the level of individual synapses. Here we identify a signaling pathway that regulates the local synthesis of proteins required to form excitatory synapses on parvalbumin-expressing (PV+) interneurons in the mouse cerebral cortex. This process involves regulation of the TSC subunit 2 (Tsc2) by the Erb-B2 receptor tyrosine kinase 4 (ErbB4), which enables local control of mRNA translation in a cell type-specific and synapse type-specific manner. Ribosome-associated mRNA profiling reveals a molecular program of synaptic proteins downstream of ErbB4 signaling required to form excitatory inputs on PV+ interneurons. Thus, specific connections use local protein synthesis to control synapse formation in the nervous system.

2022-11-24 | GSE214258 | GEO

Protein local synthesis at synapse is required for neuromuscular transmission

Project description:Protein local synthesis at synapse is required for neuromuscular transmission

| PRJNA998037 | ENA

Regulated local synthesis of ribosomal proteins maintains ribosome function in axons

Project description:Regulated local synthesis of ribosomal proteins maintains ribosome function in axons

| PRJNA559103 | ENA

Cortical wiring by synapse type-specific control of local protein synthesis

Project description:Cortical wiring by synapse type-specific control of local protein synthesis

| PRJNA884646 | ENA

GRHL2 and AP2a coordinate early surface ectoderm lineage commitment and craniofacial development (Multiome)

Project description:GRHL2 and AP2a coordinate early surface ectoderm lineage commitment and craniofacial development (Multiome)

| PRJNA812874 | ENA

GRHL2 and AP2a coordinate early surface ectoderm lineage commitment and craniofacial development [H9_d7_HiChIP_AP2KO]

Project description:GRHL2 and AP2a coordinate early surface ectoderm lineage commitment and craniofacial development [H9_d7_HiChIP_AP2KO]

| PRJNA938042 | ENA

LARP1 senses free ribosomes to coordinate supply and demand of ribosomal proteins

Project description:Terminal oligopyrimidine motif-containing (TOP) mRNAs encode all ribosomal proteins in mammals and are regulated to tune ribosome synthesis to cell state. Previous studies implicate LARP1 in 40S- or 80S-ribosome complexes that repress and stabilize TOP mRNAs. However, a mechanistic understanding of how LARP1 and TOP mRNAs interact with ribosomes to coordinate TOP mRNA outcomes is lacking. Here, we show that LARP1 senses the cellular supply of ribosomes by directly binding non-translating 80S ribosomes. Cryo-EM structures reveal a previously uncharacterized domain of LARP1 bound to and occluding the 40S mRNA channel and mutations at the LARP1-ribosome interface block formation of the 40S/80S-LARP1-TOP complexes. Free cytosolic ribosomes induce sequestration of TOP mRNAs in repressed 80S-LARP1-TOP complexes independent of alterations in mTOR signaling. Together, this work demonstrates a ribosome-sensing function of LARP1 that allows it to tune ribosome protein synthesis to the availability of free ribosomes.

2023-10-28 | GSE246077 | GEO

Identification of glycosyltransferases and glycosydases responsible for the synthesis/degradation of mucin O-glycans at the human ocular surface epithelium

Project description:The major focus of Dr. Argueso's research is to characterize the carbohydrate portion of the different mucins expressed by the ocular surface epithelia as well as the enzymes involved with their synthesis, and to determine whether the alteration of mucin glycosylation is associated with ocular surface disease.

2011-03-02 | GSE27593 | GEO

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

Tweets

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data