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      Chlamydia trachomatis inclusion membrane protein CT228 recruits elements of the myosin phosphatase pathway to regulate release mechanisms.

      Cell Reports
      Amino Acid Sequence, Chlamydia trachomatis, genetics, metabolism, HeLa Cells, Humans, Membrane Proteins, Molecular Sequence Data, Myosin-Light-Chain Phosphatase, Phosphorylation

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          Abstract

          Chlamydia trachomatis replicates within a membrane-bound compartment termed an inclusion. The inclusion membrane is modified by the insertion of multiple proteins known as Incs. In a yeast two-hybrid screen, an interaction was found between the inclusion membrane protein CT228 and MYPT1, a subunit of myosin phosphatase. MYPT1 was recruited peripherally around the inclusion, whereas the phosphorylated, inactive form was localized to active Src-family kinase-rich microdomains. Phosphorylated myosin light chain 2 (MLC2), myosin light chain kinase (MLCK), myosin IIA, and myosin IIB also colocalized with inactive MYPT1. The role of these proteins was examined in the context of host-cell exit mechanisms (i.e., cell lysis and extrusion of intact inclusions). Inhibition of myosin II or small interfering RNA depletion of myosin IIA, myosin IIB, MLC2, or MLCK reduced chlamydial extrusion, thus favoring lytic events as the primary means of release. These studies provide insights into the regulation of egress mechanisms by C. trachomatis. Copyright © 2013 The Authors. Published by Elsevier Inc. All rights reserved.

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          Journal
          23727243
          3700685
          10.1016/j.celrep.2013.04.027

          Chemistry
          Amino Acid Sequence,Chlamydia trachomatis,genetics,metabolism,HeLa Cells,Humans,Membrane Proteins,Molecular Sequence Data,Myosin-Light-Chain Phosphatase,Phosphorylation

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