title: There is more than one way to model an elephant. Experiment-driven modeling of the actin cytoskeleton.
abstract: Mathematical modeling has established its value for investigating the interplay of biochemical and mechanical mechanisms underlying actin-based motility. Because of the complex nature of actin dynamics and its regulation, many of these models are phenomenological or conceptual, providing a general understanding of the physics at play. But the wealth of carefully measured kinetic data on the interactions of many of the players in actin biochemistry cries out for the creation of more detailed and accurate models that could permit investigators to dissect interdependent roles of individual molecular components. Moreover, no human mind can assimilate all of the mechanisms underlying complex protein networks; so an additional benefit of a detailed kinetic model is that the numerous binding proteins, signaling mechanisms, and biochemical reactions can be computationally organized in a fully explicit, accessible, visualizable, and reusable structure. In this review, we will focus on how comprehensive and adaptable modeling allows investigators to explain experimental observations and develop testable hypotheses on the intracellular dynamics of the actin cytoskeleton.
authors: Richard D. Berlin Center for Cell Analysis and Modeling, University of Connecticut Health Center, Farmington, Connecticut, USA.
authors: Jonathon A
authors: JA
authors: Ditlev
authors: Bruce J
authors: BJ
authors: Mayer
authors: Leslie M
authors: LM
authors: Loew
mesh_terms: D008841:Actin Cytoskeleton / Q000737:chemistry* / Q000378:metabolism; D000199:Actins / Q000737:chemistry / Q000378:metabolism; D000818:Animals; D006801:Humans; D008840:Microfilament Proteins / Q000737:chemistry / Q000378:metabolism; D008954:Models, Biological
chemical_list: D000199:Actins; D008840:Microfilament Proteins