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La fosforilación específica para la mitosis de p60c-src por la proteína kinasa asociada con p34cdc2
D O Morgan1, J M Kaplan, J M Bishop
1Department of Microbiology, University of California, San Francisco 94143.
Cell
|June 2, 1989
Resumen
Una nueva proteína quinasa específica para la mitosis fosforila p60c-src en la treonina durante la división celular. Esta actividad de la quinasa está vinculada a p34cdc2, lo que sugiere que p60c-src actúa como un efector p34cdc2 en la mitosis.
Área de la Ciencia:
- Biología celular Biología celular.
- Biología Molecular Biología Molecular
- La bioquímica es la bioquímica.
Sus antecedentes:
- p60c-src, una proteína-tirosina quinasa, se somete a la fosforilación de la treonina en su región amino-terminal durante la mitosis.
- La identificación de la quinasa responsable de esta fosforilación mitótica específica es crucial para comprender la regulación del ciclo celular.
Objetivo del estudio:
- Para identificar y caracterizar la proteína quinasa responsable de la fosforilación de la threonina específica de la mitosis de p60c-src.
- Investigar la relación entre esta actividad de la quinasa y los reguladores mitóticos conocidos, en particular p34cdc2.2.
Principales métodos:
- Se utilizaron extractos de células mitóticas de células HeLa y huevos de Xenopus para buscar la actividad de la quinasa.
- Se realizaron ensayos de fosforilación in vitro con p60c-src purificado.
- Se empleó cartografía tríptica de fosfopéptidos para analizar los sitios de fosforilación.
- La cromatografía de filtración por gel se utilizó para evaluar la comigración de la quinasa.
- Se realizó inmunodepleción utilizando anticuerpos contra p34cdc2.
Principales resultados:
- Se identificó una actividad de proteína quinasa específica para la mitosis en células HeLa y huevos de Xenopus capaces de fosforilar p60c-src en residuos de treonina in vitro.
- El mapeo de fosfopéptidos confirmó que la quinasa identificada fosforila los mismos sitios que los modificados in vivo durante la mitosis.
- La actividad mitótica de la HeLa quinasa se combinó con la histona H1 quinasa p34cdc2-asociada.
- Los anticuerpos contra p34cdc2 agotaron la actividad de fosforilación p60c-src de los extractos mitóticos.
Conclusiones:
- Los resultados identifican una nueva quinasa específica para la mitosis que fosforila p60c-src en la threonina.
- Esta actividad de la quinasa está asociada con p34cdc2, lo que sugiere un vínculo funcional.
- p60c-src puede funcionar como un efector de p34cdc2 en procesos mitóticos específicos, contribuyendo a la regulación del ciclo celular.
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