Septins as key regulators of actin based processes in bacterial infection.
Summary of "Septins as key regulators of actin based processes in bacterial infection."
Abstract Many pathogens have evolved a variety of mechanisms to exploit the host-cell actin cytoskeleton during infection, either to enter into cells or to move within cells. These events have been investigated and documented in detail. Yet, a complete picture of the molecules and mechanisms regulating entry and intracellular movement remains to be established. Here we present a series of studies revealing that in addition to actin rearrangements the host cell also employs septins, a relatively newly characterized component of the cell cyto-skeleton, to regulate bacterial entry and restrict the dissemination of cytosolic bacteria. The challenge now is to decipher the precise role of septins during actin rearrangements and how these different cytoskeleton components orchestrate infection processes.
Affiliation
Institut Pasteur, Unité des Interactions Bactéries-Cellules, F-75015 Paris, France.
Journal Details
This article was published in the following journal.
Name: Biological chemistry
ISSN: 1437-4315
Pages:
Links
- PubMed Source: http://www.ncbi.nlm.nih.gov/pubmed/21749282
- DOI: http://dx.doi.org/10.1515/BC.2011.078
Medical and Biotech [MESH] Definitions
Septins
A family of GTP-binding proteins that were initially identified in YEASTS where they were shown to initiate the process of septation and bud formation. Septins form into hetero-oligomeric complexes that are comprised of several distinct septin subunits. These complexes can act as cytoskeletal elements that play important roles in CYTOKINESIS, cytoskeletal reorganization, BIOLOGICAL TRANSPORT, and membrane dynamics.
Actin Depolymerizing Factors
A family of low MOLECULAR WEIGHT actin-binding proteins found throughout eukaryotes. They remodel the actin CYTOSKELETON by severing ACTIN FILAMENTS and increasing the rate of monomer dissociation.
Cortactin
A microfilament protein that interacts with F-ACTIN and regulates cortical actin assembly and organization. It is also an SH3 DOMAIN containing phosphoprotein, and it mediates tyrosine PHOSPHORYLATION based SIGNAL TRANSDUCTION by PROTO-ONCOGENE PROTEIN PP60(C-SRC).
Capz Actin Capping Protein
An actin capping protein that binds to the barbed-ends of ACTIN filaments. It is a heterodimer consisting of an alpha and a beta subunit. It regulates actin assembly by stabilizing actin oligomers for elongation. In SKELETAL MUSCLE, CapZ is localized to the Z-disk.
Actin Capping Proteins
Actin capping proteins are cytoskeletal proteins that bind to the ends of ACTIN FILAMENTS to regulate actin polymerization.
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