Publication Date:
2012-06-02
Description:
Interacting sets of actin assembly factors work together in cells, but the underlying mechanisms have remained obscure. We used triple-color single-molecule fluorescence microscopy to image the tumor suppressor adenomatous polyposis coli (APC) and the formin mDia1 during filament assembly. Complexes consisting of APC, mDia1, and actin monomers initiated actin filament formation, overcoming inhibition by capping protein and profilin. Upon filament polymerization, the complexes separated, with mDia1 moving processively on growing barbed ends while APC remained at the site of nucleation. Thus, the two assembly factors directly interact to initiate filament assembly and then separate but retain independent associations with either end of the growing filament.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3613992/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉 〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3613992/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Breitsprecher, Dennis -- Jaiswal, Richa -- Bombardier, Jeffrey P -- Gould, Christopher J -- Gelles, Jeff -- Goode, Bruce L -- GM083137/GM/NIGMS NIH HHS/ -- GM43369/GM/NIGMS NIH HHS/ -- GM81648/GM/NIGMS NIH HHS/ -- R01 GM063691/GM/NIGMS NIH HHS/ -- R01 GM081648/GM/NIGMS NIH HHS/ -- R01 GM083137/GM/NIGMS NIH HHS/ -- R01 GM098143/GM/NIGMS NIH HHS/ -- R37 GM043369/GM/NIGMS NIH HHS/ -- T32 EB009419/EB/NIBIB NIH HHS/ -- T32 GM007596/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2012 Jun 1;336(6085):1164-8. doi: 10.1126/science.1218062.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Brandeis University, Waltham, MA 02454, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22654058" target="_blank"〉PubMed〈/a〉
Keywords:
Actin Cytoskeleton/*metabolism
;
Actins/chemistry/*metabolism
;
Adaptor Proteins, Signal Transducing/chemistry/*metabolism
;
Adenomatous Polyposis Coli Protein/chemistry/*metabolism
;
Animals
;
Microscopy, Fluorescence
;
Peptide Fragments/chemistry/metabolism
;
Profilins/metabolism
;
Protein Binding
;
Protein Interaction Domains and Motifs
;
Protein Multimerization
;
Rabbits
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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