Distribution and functions of kinectin isoforms.

Kinectin is an integral transmembrane protein on the endoplasmic reticulum, binding to kinesin, interacting with Rho GTPase and anchoring the translation elongation factor-1 complex. There has been debate on the specific role(s) of kinectin in different species and cell types. Here we identified 15 novel kinectin isoforms in the mouse nervous system, constituting a family of alternatively spliced carboxyl-terminal variants.

Cloning of rat telomerase catalytic subunit functional domains, reconstitution of telomerase activity and enzymatic profile of pig and chicken tissues.

Telomerase is a ribonucleoprotein polymerase which adds TTAGGG repeats to telomeric ends. Recent studies reported the reverse transcription enzyme activity mostly from the catalytic subunit (TERT) of the enzyme complex. Both human telomerase catalytic subunit (hTERT) and mouse telomerase catalytic subunit (mTERT) had been previously cloned but not rat telomerase catalytic subunit rTERT.

Kinectin anchors the translation elongation factor-1 delta to the endoplasmic reticulum.

Kinectin has been proposed to be a membrane anchor for kinesin on intracellular organelles. A kinectin isoform that lacks a major portion of the kinesin-binding domain does not bind kinesin but interacts with another resident of the endoplasmic reticulum, the translation elongation factor-1 delta (EF-1 delta). This was shown by yeast two-hybrid analysis and a number of in vitro and in vivo assays.