Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Novel phosphorylation substrates reveal a spatially regulated role for AAK1 in cell migration - SILAC proteome profiling to determine the impact of acute AAK1/BMP2K inhibition

ABSTRACT: NAKs (Numb-associated kinases) are a relatively unexplored kinase family that interacts with the endocytic machinery. Among NAK members, AAK1 has been linked to disorders such as neuropathic pain, schizophrenia, and Alzheimer's disease. Our goal is to better understand the cellular pathways regulated by AAK1 and its paralog BMP2K, as their only known role until now has been in endocytosis. Using SILAC labelling for whole cell proteome and phosphoproteome profiling of htert RPE cells pharmacological perturbation of these kinases, we demonstrate that acute inhibition of AAK1 and BMP2K significantly disrupts the abundance and phosphorylation of focal adhesion proteins. This indicates that AAK1 and BMP2K are involved in maintaining focal adhesions in addition to their role in endocytosis.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture

SUBMITTER: David Potesil

LAB HEAD: Zbynek Zdrahal

PROVIDER: PXD055851 | Pride | 2026-03-19

REPOSITORIES: Pride

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	5235_Exp1_138IS_DDA_MaxITauto_AGC100_incl_SILAC_A_ID_1.raw	Raw
	5235_Exp1_138IS_DDA_MaxITauto_AGC100_incl_SILAC_A_IM_1.raw	Raw
	5235_Exp1_138IS_DDA_MaxITauto_AGC100_incl_SILAC_A_T_1.raw	Raw
	5235_Exp1_138IS_DDA_MaxITauto_AGC100_incl_SILAC_B_ID_1.raw	Raw
	5235_Exp1_138IS_DDA_MaxITauto_AGC100_incl_SILAC_B_IM_1.raw	Raw

Items per page:

1 - 5 of 40

Similar Datasets

Novel phosphorylation substrates reveal a spatially regulated role for AAK1 in cell migration - LFQ proteome profiling to determine the impact of AAK1/BMP2K perturbation

Project description:NAKs (Numb-associated kinases) are a relatively unexplored kinase family that interacts with the endocytic machinery. Among NAK members, AAK1 has been linked to disorders such as neuropathic pain, schizophrenia, and Alzheimer's disease. Our goal is to better understand the cellular pathways regulated by AAK1 and its paralog BMP2K, as their only known role until now has been in endocytosis. Using the LFQ approach for whole cell proteome and phosphoproteome profiling of htert RPE cells with genetic perturbation of these kinases, we demonstrate that the double knockout (dKO) of AAK1 and BMP2K significantly disrupts the abundance and phosphorylation of focal adhesion proteins. This indicates that AAK1 and BMP2K are involved in maintaining focal adhesions in addition to their role in endocytosis.

2026-03-19 | PXD055831 | Pride

Novel phosphorylation substrates reveal a spatially regulated role for AAK1 in cell migration - AAK1 differential interactome profiling

Project description:NAKs (Numb-associated kinases) are a relatively unexplored kinase family that interacts with the endocytic machinery. Among NAK members, AAK1 has been linked to disorders such as neuropathic pain, schizophrenia, and Alzheimer's disease. Our goal is to better understand the cellular pathways regulated by AAK1 as its only known role until now has been in endocytosis. To define the AAK1 interactome in relation to focal adhesions, we compared its interactome in cells plated for 2 hours on collagen, which promotes focal adhesions, and poly-L-lysine (PLL), which does not. In collagen-plated cells, we discovered several differential AAK1 interactors involved in focal adhesions, the actin cytoskeleton, and recycling endosomes. In PLL-plated cells, there was a significant increase in actin cytoskeleton components and upregulation of the entire Arp2/3 complex as AAK1 interactors. This supports our other data showing that AAK1 is involved in focal adhesion maintenance and cell migration.

2026-03-19 | PXD055873 | Pride

Novel phosphorylation substrates reveal a spatially regulated role for AAK1 in cell migration - AAK1 C-terminal interactome profiling – batch 1

Project description:NAKs (Numb-associated kinases) are a relatively unexplored kinase family that interacts with the endocytic machinery. Among NAK members, AAK1 has been linked to disorders such as neuropathic pain, schizophrenia, and Alzheimer's disease. Our goal is to better understand the cellular pathways regulated by AAK1 as its only known role until now has been in endocytosis. Using a synthetic peptide identical to the C-terminus of AAK1, we observed an interaction with both the clathrin heavy chain and a subset of proteins containing the PDZ domain, including the newly identified AAK1 substrate, PDLIM5. This finding is significant as it reveals that AAK1 and PDLIM5 interact not only through the kinase domain of AAK1 and PDLIM5's consensus motif surrounding the threonine 290 (T290) but also through the PDZ domain of PDLIM5 binding the LIDL motif at the C-terminus of AAK1.

2026-03-19 | PXD056027 | Pride

Novel phosphorylation substrates reveal a spatially regulated role for AAK1 in cell migration - AAK1 C-terminal interactome profiling – batch 2,3

Project description:NAKs (Numb-associated kinases) are a relatively unexplored kinase family that interacts with the endocytic machinery. Among NAK members, AAK1 has been linked to disorders such as neuropathic pain, schizophrenia, and Alzheimer's disease. Our goal is to better understand the cellular pathways regulated by AAK1 as its only known role until now has been in endocytosis. Using a synthetic peptide identical to the C-terminus of AAK1, we observed an interaction with both the clathrin heavy chain and a subset of proteins containing the PDZ domain, including the newly identified AAK1 substrate, PDLIM5. This finding is significant as it reveals that AAK1 and PDLIM5 interact not only through the kinase domain of AAK1 and PDLIM5's consensus motif surrounding the threonine 290 (T290) but also through the PDZ domain of PDLIM5 binding the LIDL motif at the C-terminus of AAK1.

2026-03-19 | PXD056013 | Pride

Novel phosphorylation substrates reveal a spatially regulated role for AAK1 in cell migration - AAK1 interactome profiling

Project description:NAKs (Numb-associated kinases) are a relatively unexplored kinase family that interacts with the endocytic machinery. Among NAK members, AAK1 has been linked to disorders such as neuropathic pain, schizophrenia, and Alzheimer's disease. Our goal is to better understand the cellular pathways regulated by AAK1 as its only known role until now has been in endocytosis. Using the co-immunoprecipitation technique, we discovered new AAK1 interactors. These include proteins involved in the actin cytoskeleton, such as members of the Arp2/3 complex and various actin types, as well as proteins involved in cell junctions, such as the SRC kinase and RAC1. This indicates that AAK1 has additional roles beyond its previously described function in endocytosis.

2026-03-19 | PXD055980 | Pride

Novel phosphorylation substrates reveal a spatially regulated role for AAK1 in cell migration – PDLIM5 differential interactomics

Project description:PDLIM5 is a poorly explored protein, that has been shown to play a role in the maintenance of focal adhesions, likely through its interaction with actin. Our experiments demonstrate that AAK1 phosphorylates PDLIM5 on threonine 290 (T290). The aim of this experiment is to investigate the role of this phosphorylation in PDLIM5’s interaction with focal adhesions. We used co-immunoprecipitation to analyze the interactome of PDLIM5 under physiological conditions. Additionally, we compared its interactome between in wild-type (WT) cells, where it is phosphorylated by AAK1 on T290, and in AAK1 knockout (KO) cells, where it is not. This approach allowed us to compare the PDLIM5 interactome under these two conditions. We discovered that in the absence of AAK1, PDLIM5 interacts more with focal adhesion proteins such as ILK, IQGAP1, and filamins A and B. In the presence of AAK1, PDLIM5 interacts significantly more with various nuclear proteins.

2026-03-19 | PXD055912 | Pride

CDK7-CDK11 axis in spliceosome regulation and pre-mRNA splicing – phosphopeptides dataset

Project description:Cyclin-dependent kinase 11 (CDK11) is essential for the regulation of pre-mRNA splicing via phosphorylation of the core spliceosome component SF3B1. This phosphorylation is a marker of the catalytically active spliceosomes thus it is important to identify the mechanisms that regulate CDK11 itself. Here, we report that a small subset of CDK11 is phosphorylated on the activation T-loop threonine 595 (Thr595) and is associated with the activated spliceosome on chromatin in gene bodies. Mutational analyses revealed that Thr595 is essential for the formation of the active CDK11 complex with cyclin L and SAP30BP. CDK11 transiently associates with CDK7, a transcriptional kinase that also promotes the activation of other CDKs. Inhibition of CDK7 initially decreases transcription, but longer durations of inhibition lead to production of unspliced pre-mRNAs. The onset of the CDK7-mediated splicing defect correlates with the sequential dephosphorylation of CDK11 Thr595 and SF3B1. SILAC-based phosphoproteomics upon brief CDK11 inhibition identified SF3B1, CDC5L and ESS2 as CDK11 substrates, which overlap with the previously identified CDK7 substrates in the spliceosome. In summary, our study suggests that CDK7 likely acts via CDK11 Thr595 phosphorylation to regulate pre-mRNA splicing in cells. The identification of additional CDK11 substrates points to its broader role in spliceosome regulation.

2025-12-29 | PXD062535 | Pride

RNAseq results of Aeromonas dhakensis AAK1, uvrY mutant and uvrY complement

Project description:RNAseq results of Aeromonas dhakensis AAK1, uvrY mutant and uvrY complement

| PRJNA541173 | ENA

SGC-AAK1-1: A Chemical Probe Targeting AAK1 and BMP2K.

Project description:Inhibitors based on a 3-acylaminoindazole scaffold were synthesized to yield potent dual AAK1/BMP2K inhibitors. Optimization furnished a small molecule chemical probe (SGC-AAK1-1, 25) that is potent and selective for AAK1/BMP2K over other NAK family members, demonstrates narrow activity in a kinome-wide screen, and is functionally active in cells. This inhibitor represents one of the best available small molecule tools to study the functions of AAK1 and BMP2K.

| S-EPMC7073879 | biostudies-literature

Analysis of HeLa cells after transfection with miR-1, miR-124 and miR-181.

Project description:Analysis of HeLa cells at 24 hours after transfection with wild type miR-1, miR-124, miR-181 versus control transfected HeLa cells. Results were compared to protein down-regulation at 48 hours measured by SILAC-MS. Analysis of HeLa cells at 24 hours after transfection with wild type miR-1, miR-124, miR-181 versus control transfected HeLa cells. Results were compared to protein down-regulation at 48 hours measured by SILAC-MS.

2010-05-25 | E-GEOD-11968 | biostudies-arrayexpress

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