Contribution of actin to the structure of the cytoplasmic matrix

THOMAS P. STOSSELHematologylOncology Unit, Massachusetts GeneralHospital, DepartmentofMedicine, HarvardMedicalSchool, Boston, MA02114The realization that actin is aconstituentofnonmuscle cells(1) and the identification ofactin filaments in theperipheryofsuchcells (2) openedupanewworldofmolecularbiology.For the first time it became possible to explain in detail abodyofphenomenadescribed overtwocenturies concerningimportant aspects ofcell shape, movement, andconsistency.Although actin comprises only one of several intracellularfiber systems ofcells, it is anextremely important one. Thisessaybriefly reviews some present conceptsofthe contribu-tionofactin tothe"cytoplasmicmatrix."The appreciation of actin's existence in nonmuscle cellsimmediately provided some intuitively attractive ideas con-cerning the behavior ofsuch cells. First, actin is a globularmonomerthatassembles reversibly to form long fibers, andthis assembly increases the apparent viscosity of an actinsolution (3). Therefore, changes in the state ofassembly indifferent parts of a cell could account for differences incytoplasmic consistency. Second, long actin fibers, if suffi-ciently stiff and especially if organized as bundles, couldmaintainthecell orpartsofcells in aparticularconfiguration.Third, actin, workingtogether with myosin, could generatethe contractility observed in these cells. Fourth, actin fiberscouldactascablestotiepartsofthecell,includingitsinvestingmembrane, together. Thesefourbasic ideas, which concern"mechanical" properties of actin fibers, continue in theirbroadestsenseto bevalid. However,it hasbecomeapparentthatthe functionsofactin, influencedbyaseemingly endlessnumberof"actin-bindingproteins," areextraordinarily com-plex. Althoughthis complexityseemsformidableandconfus-ingat first glance, it actually is atestimony to themarvellousversatilityofthis highlyconserved protein(4) andtonature'singenuity in theengineering ofcytoplasm.Research on actin in cytoplasmic structure and functionhasbeenadvancing ontwofronts. Onone,investigatorsstudythe details ofactin assembly and rheology in vitro andtheinfluence ofpurified actin-associated proteinson these prop-erties. Therheological behaviorofcrudecytoplasmic extractshas often provided the direction for such research. On theother, cell biologists examinethemorphologyofactin incellsin thelight andthe electron microscope and also determinethe location ofthe actin-associated proteinsin thecell.

• Publication year

  1984

• Venue

  Journal of Cell Biology

• Publication date

  1984-07-01

• Fields of study

  Biology, Medicine

• Identifiers
  DOI 10.1083/JCB.99.1.15SPMID 6086665PMCID 2275585
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

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