Abstract
Microtubule-associated protein 1A (MAP1A) and MAP1B are developmentally regulated proteins linked to axon formation. They each consist of a unique heavy chain and three common light chains. We used immunofluorescence microscopy to qualitatively assess the variability in MAP1 subunit expression between individual cells. The ratio of light chain 1 to MAP1 heavy chain varies greatly between cells with some cells expressing MAP1A heavy chain in the apparent absence of light chain 1. The results imply the existence of MAP1 molecules that differ in light chain composition. Transfection experiments indicate that the light chains differ in microtubule binding activity and subcellular targeting activity. This further suggests that the regulation of MAP1 light chain content can control MAP1 function.
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