Fig. 6: Integrin α1 (ITGA1) activates TCPTP by displacing the TCPTP autoinhibitory domain. | Nature Communications

Fig. 6: Integrin α1 (ITGA1) activates TCPTP by displacing the TCPTP autoinhibitory domain.

From: The catalytic activity of TCPTP is auto-regulated by its intrinsically disordered tail and activated by Integrin alpha-1

Fig. 6

a EC50 assays of ITGA1 peptides vs TCPTP, monitored by dephosphorylation of pEGFR peptide-1 as substrate derived from the EGFR cytoplasmic tail. Data are presented as the mean of three independent reactions (n = 3; mean ± SE). b Overlay of the 2D [1H,15N] TROSY spectra of (2H,15N)-labeled TCPTPCAT (black) and in complex with ITGA1_FCT (orange). Residues with CSPs are annotated. c CSP comparison for residues in TCPTPCAT loops L1, L2, L6 and L14 (colored as in Fig. 3e) when in complex with either TCPTPTailRK, ITGA1_FCT or ITGA1_TR peptides. d Catalytic activity of TCPTP and TCPTPCAT (residues 1–314) in the presence or absence of ITGA1 peptides (ITGA1_TR or ITGA1_FCT); same substrate as described in a. Data are presented as the mean of nine independent reactions (n = 9; mean ± SE). Source data are provided as a Source Data file.

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