Fig. 3: A natively localized variant of PTP1BPS.
From: Minimally disruptive optical control of protein tyrosine phosphatase 1B
a We assembled PTP1BPS* and PTP1BPS** by attaching residues 299–405 (the disordered proline-rich region) and 299–435 (the proline-rich region and ER anchor), respectively, of full-length PTP1B to the C-terminus of PTP1BPS. Colors correspond to the catalytic domain of PTP1B (orange), the LOV2 domain (blue), the proline-rich region of PTP1B (black), and the ER anchor of PTP1B (gray). b PTP1BPS* is photoswitchable but exhibits a reduced DR, relative to PTP1BPS; mutations that stabilize the Jα helix do not improve DR. The plotted data depict the mean, SE, and associated estimates of DR for n = 6 independent experiments. c Saturation curves show the activity of PTP1BPS* on pNPP (kcat-dark/kcat-light = 2.03 ± 0.04). Error bars denote SE for n = 3 independent reactions. d Images of COS-7 cells expressing GFP-tagged variants of PTP1B. PTP1B435 and PTP1BPS** exhibit indistinguishable localization patterns (scale bars appear as a white line over a small black rectangle in the lower right corner of each image; 10 μm). Source data are provided as a Source Data file.
