The distance that kinesin-1 holds its cargo from the microtubule surface measured by fluorescence interference contrast microscopy.

ABSTRACT: Kinesin-1 is a motor protein that carries cellular cargo such as membrane-bounded organelles along microtubules (MTs). The homodimeric motor molecule contains two N-terminal motor domains (the motor "heads"), a long coiled-coil domain (the "rod" or "stalk"), and two small globular "tail" domains. Much has been learned about how kinesin's heads step along a MT and how the tail is involved in cargo binding and autoinhibition. However, little is known about the role of the rod. Here, we investigate the extension of the rod during active transport by measuring the height at which MTs glide over a kinesin-coated surface in the presence of ATP. To perform height measurements with nanometer precision, we used fluorescence interference contrast microscopy, which is based on the self-interference o

SUBMITTER: Kerssemakers J 

PROVIDER: S-EPMC1595308 | biostudies-literature | 2006 Oct

REPOSITORIES: biostudies-literature