Unknown

Dataset Information

0

Porcine myosin-VI: characterization of a new mammalian unconventional myosin.


ABSTRACT: We have cloned a new mammalian unconventional myosin, porcine myosin-VI from the proximal tubule cell line, LLC-PK1 (CL4). Porcine myosin-VI is highly homologous to Drosophila 95F myosin heavy chain, and together these two myosins comprise a sixth class of myosin motors. Myosin-VI exhibits ATP-sensitive actin-binding activities characteristic of myosins, and it is associated with a calmodulin light chain. Within LLC-PK1 cells, myosin-VI is soluble and does not associate with the major actin-containing domains. Within the kidney, however, myosin-VI is associated with sedimentable structures and specifically locates to the actin- and membrane-rich apical brush border domain of the proximal tubule cells. This motor was not enriched within the glomerulus, capillaries, or distal tubules. Myosin-VI associates with the proximal tubule cytoskeleton in an ATP-sensitive fashion, suggesting that this motor is associated with the actin cytoskeleton within the proximal tubule cells. Given the difference in association of myosin-VI with the apical cytoskeleton between LLC-PK1 cells and adult kidney, it is likely that this cell line does not fully differentiate to form functional proximal tubule cells. Myosin-VI may require the presence of additional elements, only found in vivo in proximal tubule cells, to properly locate to the apical domain.

SUBMITTER: Hasson T 

PROVIDER: S-EPMC2120210 | biostudies-other | 1994 Oct

REPOSITORIES: biostudies-other

altmetric image

Publications

Porcine myosin-VI: characterization of a new mammalian unconventional myosin.

Hasson T T   Mooseker M S MS  

The Journal of cell biology 19941001 2


We have cloned a new mammalian unconventional myosin, porcine myosin-VI from the proximal tubule cell line, LLC-PK1 (CL4). Porcine myosin-VI is highly homologous to Drosophila 95F myosin heavy chain, and together these two myosins comprise a sixth class of myosin motors. Myosin-VI exhibits ATP-sensitive actin-binding activities characteristic of myosins, and it is associated with a calmodulin light chain. Within LLC-PK1 cells, myosin-VI is soluble and does not associate with the major actin-cont  ...[more]

Similar Datasets

| S-EPMC4469105 | biostudies-literature
| S-EPMC8924246 | biostudies-literature
| S-EPMC2543112 | biostudies-literature
| S-EPMC4792956 | biostudies-literature
| S-EPMC9273875 | biostudies-literature
2020-05-31 | GSE149448 | GEO
| S-EPMC38240 | biostudies-other
| S-EPMC1201382 | biostudies-literature
| S-EPMC6673701 | biostudies-literature
| S-EPMC2064848 | biostudies-literature