PMID- 10209028
OWN - NLM
STAT- MEDLINE
DCOM- 19990517
LR  - 20190508
IS  - 0021-9525 (Print)
IS  - 0021-9525 (Linking)
VI  - 145
IP  - 2
DP  - 1999 Apr 19
TI  - Relationship between Arp2/3 complex and the barbed ends of actin filaments at the
      leading edge of carcinoma cells after epidermal growth factor stimulation.
PG  - 331-45
AB  - Using both light and high resolution electron microscopy, we analyzed the spatial
      and temporal relationships between the Arp2/3 complex and the nucleation activity
      that is required for lamellipod extension in mammary carcinoma cells after
      epidermal growth factor stimulation. A rapid two- to fourfold increase in
      filament barbed end number occurs transiently after stimulation and remains
      confined almost exclusively to the extreme outer edge of the extending lamellipod
      (within 100-200 nm of the plasma membrane). This is accompanied by an increase in
      filament density at the leading edge and a general decrease in filament length,
      with a specific loss of long filaments. Concomitantly, the Arp2/3 complex is
      recruited with a 1.5-fold increase throughout the entire cortical filament
      network extending 1-1.5 microm in depth from the membrane at the leading edge.
      The recruitment of the Arp2/3 complex at the membrane of the extending lamellipod
      indicates that Arp2/3 may be involved in initial generation of growing filaments.
      However, only a small subset of the complex present in the cortical network
      colocalizes near free barbed ends. This suggests that the 100-200-nm
      submembraneous compartment at the leading edge of the extending lamellipod
      constitutes a special biochemical microenvironment that favors the generation and
      maintenance of free barbed ends, possibly through the locally active Arp2/3
      complex, severing or decreasing the on-rate of capping protein. Our results are
      inconsistent with the hypothesis suggesting uncapping is the dominant mechanism
      responsible for the generation of nucleation activity. However, they support the 
      hypothesis of an Arp2/3-mediated capture of actin oligomers that formed close to 
      the membrane by other mechanisms such as severing. They also support pointed-end 
      capping by the Arp2/3 complex, accounting for its wide distribution at the
      leading edge.
FAU - Bailly, M
AU  - Bailly M
AD  - Department of Anatomy and Structural Biology, Albert Einstein College of
      Medicine, Bronx, New York 10461, USA. bailly@aecom.yu.edu
FAU - Macaluso, F
AU  - Macaluso F
FAU - Cammer, M
AU  - Cammer M
FAU - Chan, A
AU  - Chan A
FAU - Segall, J E
AU  - Segall JE
FAU - Condeelis, J S
AU  - Condeelis JS
LA  - eng
PT  - Journal Article
PT  - Research Support, U.S. Gov't, Non-P.H.S.
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 (Actin-Related Protein 2)
RN  - 0 (Actin-Related Protein 3)
RN  - 0 (Actins)
RN  - 0 (Cytoskeletal Proteins)
RN  - 62229-50-9 (Epidermal Growth Factor)
SB  - IM
MH  - Actin-Related Protein 2
MH  - Actin-Related Protein 3
MH  - Actins/*metabolism
MH  - Animals
MH  - Cell Membrane/drug effects/*ultrastructure
MH  - Cell Membrane Permeability
MH  - *Cytoskeletal Proteins
MH  - Cytoskeleton/drug effects/*ultrastructure
MH  - Epidermal Growth Factor/*pharmacology
MH  - Female
MH  - Mammary Neoplasms, Experimental/pathology/*ultrastructure
MH  - Microscopy, Fluorescence
MH  - Models, Biological
MH  - Rats
PMC - PMC2133111
EDAT- 1999/04/20 00:00
MHDA- 1999/04/20 00:01
CRDT- 1999/04/20 00:00
PHST- 1999/04/20 00:00 [pubmed]
PHST- 1999/04/20 00:01 [medline]
PHST- 1999/04/20 00:00 [entrez]
AID - 10.1083/jcb.145.2.331 [doi]
PST - ppublish
SO  - J Cell Biol. 1999 Apr 19;145(2):331-45. doi: 10.1083/jcb.145.2.331.