Erratum

This article refers to:

Recent progress in tight junction modulation for improving bioavailability

Correction to: Recent progress in tight junction modulation for improving bioavailability

Saaber D, Wollenhaup S, Baumann K, Reichl S. Recent progress in tight junction modulation for improving bioavailability.

Expert Opin Drug Discov. 2014;9(4):367-381.

Following publication of this article, it an error has been identified in Figure 1. In this figure PKC is repeated twice but the red

one has to be PKA. The correct figure is given below

Figure 1. Schematic presentation of tight junction (TJ) regulation. A summary of the possible pathways of TJ regulation. Phosphorylation of the myosin light chain II leads to actin stress fiber formation and opens the TJ by its contractile forces [123,124]. This process is highly regulated by the balance between myosin light-chain kinase (MLCK) and myosin light-chain phosphatase (MLCP) [125]. A presumed mechanism for MLCP inhibition by PKC is via the small protein CPI-17 [126]. Furthermore, RhoA and its downstream effectors rho-associated protein kinases 1 and 2 can phosphorylate the myosin phosphatase targeting protein 1 subunit of MLCP [127]. Rho A, whose activity is regulated by protein kinase A (a cAMPdependent protein kinase), is a part of the superfamily of small GTPases [127]. The figure contains six examples of receptormediated TJ regulation.

AC: Adenylate cyclase; MLCK: Myosin light-chain kinase; MLCP: Myosin light-chain phosphatase (3 subunits); P: Phosphatase; PAR-2: Protease-activated receptor 2; PDE: Phosphodiesterase; PKA: Protein kinase A; PKC: Protein kinase C; ROCK: Rho-associated protein kinase; TJ: Tight junctions.