May 14, 1999FEBS LettersOpen Access

ZIP kinase identified as a novel myosin regulatory light chain kinase in HeLa cells

View Full Paper

Ask AI

Bookmark

Population

HeLa cells (cDNA library)

Design

Preclinical

Authors

Discussion

Preclinical identification of ZIPK as Ca2+-independent MRLC kinase; leaves open its relevance to cardiovascular myosin regulation in vivo.

Population

HeLa cells (cDNA library)

Intervention

Isolation and characterization of zipper-interacting protein kinase (ZIPK)

Outcome

Phosphorylation of the regulatory light chain of myosin II (MRLC) and activation of actin-activated MgATPase activitysurrogate

ZIPK is identified as the first non-muscle myosin light chain kinase that phosphorylates MRLC at two sites in a Ca2+/calmodulin independent manner.

Murata‐Hori et al. (1999) studied this question.

View Full Paper

Ask AI

Bookmark

Preclinical identification of ZIPK as Ca2+-independent MRLC kinase; leaves open its relevance to cardiovascular myosin regulation in vivo.