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

ABSTRACT: 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.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture

SUBMITTER: David Potesil

LAB HEAD: Zbynek Zdrahal

PROVIDER: PXD055912 | Pride | 2026-03-19

REPOSITORIES: Pride

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			Action	DRS
	5880_TIMS1_RSLC-74m_TFA_DIA_10_2_BA2_1_30380.d.zip	Other
	5880_TIMS1_RSLC-74m_TFA_DIA_11_BA3_1_30455.d.zip	Other
	5880_TIMS1_RSLC-74m_TFA_DIA_12_BA4_1_30511.d.zip	Other
	5880_TIMS1_RSLC-74m_TFA_DIA_13_BA5_1_30246.d.zip	Other
	5880_TIMS1_RSLC-74m_TFA_DIA_14_BA6_1_30479.d.zip	Other

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