PMID- 10087267
OWN - NLM
STAT- MEDLINE
DCOM- 19990614
LR  - 20190508
IS  - 0021-9525 (Print)
IS  - 0021-9525 (Linking)
VI  - 144
IP  - 6
DP  - 1999 Mar 22
TI  - Role of proteins of the Ena/VASP family in actin-based motility of Listeria
      monocytogenes.
PG  - 1245-58
AB  - Intracellular propulsion of Listeria monocytogenes is the best understood form of
      motility dependent on actin polymerization. We have used in vitro motility assays
      of Listeria in platelet and brain extracts to elucidate the function of the focal
      adhesion proteins of the Ena (Drosophila Enabled)/VASP (vasodilator-stimulated
      phosphoprotein) family in actin-based motility. Immunodepletion of VASP from
      platelet extracts and of Evl (Ena/VASP-like protein) from brain extracts of Mena 
      knockout (-/-) mice combined with add-back of recombinant (bacterial or
      eukaryotic) VASP and Evl show that VASP, Mena, and Evl play interchangeable roles
      and are required to transform actin polymerization into active movement and
      propulsive force. The EVH1 (Ena/VASP homology 1) domain of VASP is in slow
      association-dissociation equilibrium high-affinity binding to the
      zyxin-homologous, proline-rich region of ActA. VASP also interacts with F-actin
      via its COOH-terminal EVH2 domain. Hence VASP/ Ena/Evl link the bacterium to the 
      actin tail, which is required for movement. The affinity of VASP for F-actin is
      controlled by phosphorylation of serine 157 by cAMP-dependent protein kinase.
      Phospho-VASP binds with high affinity (0.5 x 10(8) M-1); dephospho-VASP binds
      40-fold less tightly. We propose a molecular ratchet model for insertional
      polymerization of actin, within which frequent attachment-detachment of VASP to
      F-actin allows its sliding along the growing filament.
FAU - Laurent, V
AU  - Laurent V
AD  - Dynamique du Cytosquelette, Laboratoire d'Enzymologie et Biochimie Structurales, 
      CNRS, 91198 Gif-sur-Yvette, France.
FAU - Loisel, T P
AU  - Loisel TP
FAU - Harbeck, B
AU  - Harbeck B
FAU - Wehman, A
AU  - Wehman A
FAU - Grobe, L
AU  - Grobe L
FAU - Jockusch, B M
AU  - Jockusch BM
FAU - Wehland, J
AU  - Wehland J
FAU - Gertler, F B
AU  - Gertler FB
FAU - Carlier, M F
AU  - Carlier MF
LA  - eng
GR  - R01 GM058801/GM/NIGMS NIH HHS/United States
GR  - GM 58801-01/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Cell Biol
JT  - The Journal of cell biology
JID - 0375356
RN  - 0 (Actins)
RN  - 0 (Carrier Proteins)
RN  - 0 (Cell Adhesion Molecules)
RN  - 0 (Contractile Proteins)
RN  - 0 (Cytoskeletal Proteins)
RN  - 0 (DNA Primers)
RN  - 0 (DNA-Binding Proteins)
RN  - 0 (ENA-VASP proteins)
RN  - 0 (Enah protein, mouse)
RN  - 0 (Evl protein, mouse)
RN  - 0 (Microfilament Proteins)
RN  - 0 (Phosphoproteins)
RN  - 0 (Profilins)
RN  - 0 (Proteins)
RN  - 0 (vasodilator-stimulated phosphoprotein)
SB  - IM
MH  - Actins/chemistry/*physiology/ultrastructure
MH  - Animals
MH  - Base Sequence
MH  - Binding Sites
MH  - Blood Platelets/metabolism
MH  - Brain/metabolism
MH  - Carrier Proteins/genetics/physiology
MH  - Cell Adhesion Molecules/genetics/*physiology
MH  - *Contractile Proteins
MH  - *Cytoskeletal Proteins
MH  - DNA Primers/genetics
MH  - DNA-Binding Proteins/genetics/*physiology
MH  - Listeria monocytogenes/genetics/*physiology
MH  - Mice
MH  - Mice, Knockout
MH  - Microfilament Proteins/physiology
MH  - Microscopy, Electron
MH  - Models, Biological
MH  - Movement/physiology
MH  - Phosphoproteins/genetics/*physiology
MH  - Profilins
MH  - Protein Binding
MH  - Proteins/genetics/physiology
PMC - PMC2150578
EDAT- 1999/03/24 00:00
MHDA- 1999/03/24 00:01
CRDT- 1999/03/24 00:00
PHST- 1999/03/24 00:00 [pubmed]
PHST- 1999/03/24 00:01 [medline]
PHST- 1999/03/24 00:00 [entrez]
AID - 10.1083/jcb.144.6.1245 [doi]
PST - ppublish
SO  - J Cell Biol. 1999 Mar 22;144(6):1245-58. doi: 10.1083/jcb.144.6.1245.