Fig. 1: βA1-crystallin is a binding partner of PTP1B. | Communications Biology

Fig. 1: βA1-crystallin is a binding partner of PTP1B.

From: βA1-crystallin regulates glucose metabolism and mitochondrial function in mouse retinal astrocytes by modulating PTP1B activity

Fig. 1

Representative western blot and densitometry graph from co-immunoprecipitation studies in mouse WT (a, b) or Cryba1 KO (c, d) astrocytes transfected with blank-mCherry, βA3-crystallin-mCherry (βA3-mCherry), βA1-crystallin-mCherry (βA1-mCherry), and βA3/A1-crystallin-mCherry (βA3/A1-mCherry) show interaction of PTP1B with both βA3- and βA1-crystallin; n = 4. e, f Co-immunoprecipitation assay showing βA3/A1-crystallin levels in the Co-IP eluent by western blot analysis and densitometry, indicating binding to PTP1B, upon pull down with mNeonGreen antibody-bound magnetic beads from lysates of astrocytes overexpressing PTP1B (Ad-CMV-mNeonGreen-mPtpn1) and Cryba1 (Ad-CMV-RFP-mCryba1). Pull down with mouse IgG showed no binding for βA3/A1-crystallin; n = 4. g Ribbon diagram obtained by molecular modeling showing superimposed βA1-crystallin (orange), βA3-crystallin (blue), and PTP1B (gray). Neither isoform is able to bind to the pocket of PTP1B active site (Cys215, Red). The βA1, but not the βA3 isoform (due to a steric bump of terminal extension) interacts with an allosteric binding site (green) on the surface of PTP1B.

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