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 - AAK1 C-terminal interactome profiling – batch 1

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 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.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture

SUBMITTER: David Potesil

LAB HEAD: Zbynek Zdrahal

PROVIDER: PXD056027 | Pride | 2026-03-19

REPOSITORIES: Pride

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	5489_Exp1_78IS_DIA_400-1000_10_1.raw	Raw
	5489_Exp1_78IS_DIA_400-1000_1_1.raw	Raw
	5489_Exp1_78IS_DIA_400-1000_2_1.raw	Raw
	5489_Exp1_78IS_DIA_400-1000_3_1.raw	Raw
	5489_Exp1_78IS_DIA_400-1000_4_1.raw	Raw

Items per page:

1 - 5 of 16

Similar Datasets

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 - 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 – 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

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 - SILAC proteome profiling to determine the impact of acute AAK1/BMP2K inhibition

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 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.

2026-03-19 | PXD055851 | Pride

Proteomic identification and structural basis for the interaction between sorting nexin SNX17 and PDLIM family proteins

Project description:The sorting nexin SNX17 controls endosome-to-cell surface recycling of diverse transmembrane cargo proteins including integrins, the amyloid precursor protein and lipoprotein receptors. This requires association with the multi-subunit Commander trafficking complex, which depends on the C-terminus of SNX17 through unknown mechanisms. Using affinity enrichment proteomics, we find that a C-terminal peptide of SNX17 is not only sufficient for Commander interaction but also associates with members of the actin-associated PDZ and LIM domain (PDLIM) family. We show that SNX17 contains a type III PSD95/Dlg/Zo1 (PDZ) binding motif (PDZbm) that binds specifically to the PDZ domains of PDLIM family proteins but not to other PDZ domains tested. The structure of the PDLIM7 PDZ domain bound to the SNX17 C-terminus was determined by NMR spectroscopy and reveals an unconventional perpendicular peptide interaction. Mutagenesis confirms the interaction is mediated by specific electrostatic contacts and a uniquely conserved proline-containing loop sequence in the PDLIM protein family. Our results define the mechanism of SNX17-PDLIM interaction and suggest that the PDLIM proteins may play a role in regulating the activity of SNX17 in conjunction with Commander and actin-rich endosomal trafficking domains.

2022-11-07 | PXD036424 | 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

Gene expression profile associated with the PDZ ligand-motif of HPV16-E6 oncoprotin in the skin of transgenic mice models

Project description:The K14E6 transgenic mice developskin hyperplasia,benign tumors and skin cancer. The tumor formation capacity diminishes when E6 lacks its PDZ ligand-motif. This study aims to compare the transciptional profiles of transgenic K14E6 mice with K14E6 Δ146-151 (lacking the PDZ domain) in order to explore the role of PDZ in early skin carcinogenesis. Skin tissue from three different strains of mice were dissected for RNA extraction, processing and hybridization in Affymetrix Mouse Genome 430 2,0 array. We processed three biological replicates per strain. 3 mice were used for each replicate pool for a final RNA concentration of 3 micrograms. The arrays were analyzed using Partek Genomics suite software.

2010-07-27 | E-GEOD-22417 | biostudies-arrayexpress

The HPV16-E6 oncoprotein induces the expression of Keratin-6b and 2 delays wound healing by means of its PDZ-ligand domain in vivo

Project description:The K14E6 transgenic mice develop skin hyperplasia, benign tumors, and cancer in the dorsal skin spontaneously. The E6 oncoprotein own its tumorigenic potential to a region located near the C-Terminal domain, better known as the PDZ ligand-domain. The aim of this work was to describe early cellular processes affected by the E6’s PDZ ligand-domain when is expressed in the skin of transgenic mice using microarray technology. Results. A total of 222 genes were differentially expressed (FC:1.5, Adj.p.value <0.05, and b value > 0.5) in the skin of K14E6 mice as compared to K14E6Δ146-151 mice. Out of those, 70 genes were up-regulated and 151 genes were down-regulated. Enzyme linked receptor protein signaling was the most affected process in our data, followed by cell adhesion, development, and lipid biosynthesis. We also found that the K14E6 strains induces the mRNA of the wound-inducible gene K6b, and delocalizes E-cadherin protein in the entire epidermis. Finally, CD34 and K15 epidermal stem cell marker proteins diminish its expression in the skin, in a PDZ-dependent manner. Conclusions. The PDZ ligand-domain of HPV16-E6 oncoprotein affects the expression of several genes involved in cellular processes that could be relevant in the HPV-induced carcinogenesis. Since HPV16-E6 oncoproteins lacking the PDZ ligand-domain loose its oncogenic potential, the knowledge of genes transcriptionally affected by the E6’s PDZ ligand-domain will provide valuable information about HPV-induced skin carcinogenesis.

2017-11-30 | GSE99868 | 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