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New isoforms of multifunctional calcium/calmodulin‐dependent protein kinase II
Author(s) -
Mayer Peter,
Möhlig Matthias,
Schatz Helmut,
Pfeiffer Andreas
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)80678-n
Subject(s) - gene isoform , alternative splicing , calmodulin , homology (biology) , biology , protein superfamily , protein kinase a , homologous chromosome , rna splicing , genetics , microbiology and biotechnology , kinase , biochemistry , gene , enzyme , rna
Calcium/calmodulin dependent protein kinase II (CaM kinase II) seems to act as an important regulator of intracellular signal transmission. Four subtypes, termed α to δ, have been cloned; some of them can exist as different splicing variants. All these isoforms share a great overall homology, and they contain 3 areas of low homology. We have identified 5 new variants of subtype delta so that the total number of different isoforms now adds up to 12. These variants are probably a result of different splicing and show several deletions in regard to subtype delta. The deletion sites do exactly match regions of low homology between the subtypes. This suggests a functional division of the CaM kinase II molecule into homologous and variable domains. The homologous domains are highly conserved. Therefore, it might be the case that the constitution of the variable domains is more significant for a certain isoform than its belonging to one of the 4 subtypes α to δ.