Chlamydia trachomatis Inclusion Membrane Protein CT228 Recruits Elements of the Myosin Phosphatase Pathway to Regulate Release Mechanisms
| Autor: | Ted Hackstadt, Alexandra C. Barger, Vinod Nair, Erika I. Lutter |
|---|---|
| Rok vydání: | 2013 |
| Předmět: |
Myosin light-chain kinase
Protein subunit Phosphatase Molecular Sequence Data Membrane Proteins Chlamydia trachomatis macromolecular substances Biology General Biochemistry Genetics and Molecular Biology Article Cell biology Myosin Phosphatase Pathway Myosin-Light-Chain Phosphatase Membrane protein lcsh:Biology (General) Myosin Phosphorylation Humans Myosin-light-chain phosphatase Amino Acid Sequence lcsh:QH301-705.5 HeLa Cells |
| Zdroj: | Cell Reports, Vol 3, Iss 6, Pp 1921-1931 (2013) |
| ISSN: | 2211-1247 |
| DOI: | 10.1016/j.celrep.2013.04.027 |
| Popis: | SummaryChlamydia 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. |
| Databáze: | OpenAIRE |
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