Mechanism and function of formins in the control of actin assembly.
By B. L. Goode, M. Eck. Annual Review of Biochemistry, 2007
842 citations recorded by the source corpus.
Subfields: Cardiology and Cardiovascular Medicine, Cell Biology
View Paper: https://www.semanticscholar.org/paper/9dbc14ddef3f18fe57799824da20b1590f09305a
How researchers see this paper
The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.
In Cardiology and Cardiovascular Medicine
In Cell Biology
- R. Grosse
- R. Dominguez
- L. A. Lowery
- P. Lappalainen
- David Van Vactor
- K. Holmes
- Oliver T. Fackler
- P. Mattila
Citations in the corpus
- Cell motility through plasma membrane blebbing (2008, background): “Beyond this ability to nucleate actin fi laments, some diaphanous formins can also regulate bundling of actin fi laments ( Faix and Grosse, 2006 ; Goode and Eck, 2007 ) or amplify Rho-ROCK signaling ( Kitzing et al., 2007 ), functions that could be at work during bleb contraction.”
- Filopodia: molecular architecture and cellular functions (2008, background): “Formins comprise a large protein family that induces the formation of unbranched actin filaments by processive barbed-end nucleation and elongatio”
- Tissue Stiffness Dictates Development, Homeostasis, and Disease Progression (2015, background): “ROCK is a serine/threonine kinase that can phosphorylate a variety of substrates, including the myosin-binding subunit of myosin phosphatase and myosin regulatory light chain, to stimulate crosslinking of actin by myosin and enhance actomyosin contractility,(16) whereas mDia catalyzes actin nucleati”
- Actin Structure and Function (2011, positive): “Formins are unique among actin filament nucleators in that they use the FH2 domain for interaction with actin and promote not only nucleation, but also processive barbed-end elongation (19).”
- The trip of the tip: understanding the growth cone machinery (2009, background): “Downstream of Rho GTPase signalling, formins nucleate and then remain continuously associated with elongating F-actin barbed end”
- Actin dynamics, architecture, and mechanics in cell motility. (2014, background): “The FH1 domain is an unstructured domain that acts as a lasso to rope in profilinactin molecules while the FH2 domain interacts with the barbed ends of actin filaments (60, 104).”
- Amiloride inhibits macropinocytosis by lowering submembranous pH and preventing Rac1 and Cdc42 signaling (2010, neutral): “mediated by Arp2/3 (Condeelis, 2001) or formins (Goode and Eck, 2007).”