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Open AccessDissertation10.31274/rtd-180813-11093

The interaction between actin filaments and the cytoskeleton-membrane attachment site protein talin

Jinwen Zhang-1995-01-01

TL;DRAbstract

Talin, a protein localized primarily in cell-matrix type adherens junctions, is involved in linking the cytoskeleton to the cell membrane. The major objectives of my study were to (1) determine the structural basis for the effect of pH and ionic strength on the direct talin-actin interaction, (2) examine the effects of other factors, such as specific phospholipids, on the talin-actin interaction, and (3) compare abilities of human platelet and avian smooth muscle talins to interact with actin. Negative staining results showed that at pH 6.4 and low ionic strength, talin extensively crosslinked actin filaments into both tight networks and bundles. Some of the bundles consisted of parallel actin filaments with an interfilament spacing of -13 nm, and talin crossbridges spaced at ~ 36 nm intervals along the actin bundles. As pH and/or ionic strength was increased, talin's actin bundling activity was decreased first, then its networking activity. Chemical crosslinking indicated that talin w

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Talin, a protein localized primarily in cell-matrix type adherens junctions, is involved in linking the cytoskeleton to the cell membrane. The major objectives of my study were to (1) determine the structural basis for the effect of pH and ionic strength on the direct talin-actin interaction, (2) examine the effects of other factors, such as specific phospholipids, on the talin-actin interaction, and (3) compare abilities of human platelet and avian smooth muscle talins to interact with actin. Negative staining results showed that at pH 6.4 and low ionic strength, talin extensively crosslinked actin filaments into both tight networks and bundles. Some of the bundles consisted of parallel actin filaments with an interfilament spacing of -13 nm, and talin crossbridges spaced at ~ 36 nm intervals along the actin bundles. As pH and/or ionic strength was increased, talin's actin bundling activity was decreased first, then its networking activity. Chemical crosslinking indicated that talin w

Keywords

ActinMicrofilamentCytoskeletonChemistryBiophysicsActin remodelingActin cytoskeletonMDia1

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