Interaction of calmodulin and a calmodulin-binding peptide from myosin light chain kinase: major spectral changes in both occur as the result of complex formation

Klevit, Rachel E.; Blumenthal, Donald K.; Wemmer, David E.; Krebs, Edwin G.

doi:10.1021/bi00348a047

Cited by 134 publications

(80 citation statements)

References 24 publications

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“…To date, only the CaM-regulatory region of myosin light chain kinase has been characterized in detail (6)(7)(8)(9).…”

mentioning

confidence: 99%

“…Limited proteolysis and chemical labeling studies suggest that the human erythrocyte enzyme contains discrete domains involved in membrane association (30)(31)(32)(33)(34)(35), catalysis (81 kDa), and CaM regulation (8)(9)(10). Attempts to isolate and characterize these domains, particularly that containing the CaM-regulatory region, by conventional biochemical techniques have been uniformly unsuccessful in this and other laboratories.…”

mentioning

confidence: 99%

See 1 more Smart Citation

A C-terminal, calmodulin-like regulatory domain from the plasma membrane Ca2+-pumping ATPase.

Brandt

Zurini

Neve

et al. 1988

Proc. Natl. Acad. Sci. U.S.A.

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A cDNA that encodes what appears to be the inhibitory domain of the plasma membrane calcium-pumping ATPase (Ca2+-ATPase) has been isolated by screening a Agtll bovine brain cDNA library with antibodies prepared against the human erythrocyte membrane Ca2 + -ATPase. This screening resulted in isolation of a bacteriophage containing a 1.5-kilobase cDNA insert encoding a 71-residue polypeptide, the remainder being a large 3' terminal noncoding region. A portion of this deduced peptide sequence was identical to that of a peptide isolated from a V8 protease digest of the human erythrocyte Ca2+-ATPase except for 1 residue. Antibodies purified by immunoabsorption to the fusion protein containing this cDNA-encoded polypeptide reacted only with those fragments of a limited trypsin digest of the human erythrocyte Ca2+-ATPase that contain the inhibitory domain. Moreover, these antibodies were able to partially stimulate basal enzyme activity and block further activation by calmodulin. The encoded polypeptide bears homology to the glutamic acid-rich regions N-terminal to the Ca2+-binding loops of calmodulin and to a lesser extent with the loops themselves. This encoded polypeptide also represents the C terminus of the Ca2+-ATPase. Portions of the isolated cDNA were homologous to the 3' noncoding region of the sarcoplasmic reticulum Ca2+-ATPase cDNA, indicating a possible mechanism for the evolution of these distinct membrane Ca2+ pumps.

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“…To date, only the CaM-regulatory region of myosin light chain kinase has been characterized in detail (6)(7)(8)(9).…”

mentioning

confidence: 99%

mentioning

confidence: 99%

A C-terminal, calmodulin-like regulatory domain from the plasma membrane Ca2+-pumping ATPase.

Brandt

Zurini

Neve

et al. 1988

Proc. Natl. Acad. Sci. U.S.A.

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“…However, the spectrum shape is very reproducible among the hybrid sequence peptides, and seems to be indicative of the folded core structure (Pease, et al, 1990). The 8222 observed corresponds to approximately 47% of the peptide being helical at 1 0°C (Kievit, et al, 1985). If this hell city is attributed only to the helical region 0 0 .…”

Section: Peptide Foldingmentioning

confidence: 89%

Structures and related properties of helical, disulfide-stabilized peptides

Pagel

1993

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“…On a more general line, this then suggests that complementary residues in CaM and the CaM-binding domain of targets are important for efficient (i. e. high-affinity) interaction. Recent NMR work on the interaction of CaM with a synthetic peptide corresponding to the CaM-binding region of skeletal muscle myosin light-chain kinase [17] points to the importance of the central helix of CaM, which includes the cluster of Glu residues 82 -84 (e. g. see [S]). This is also in line with recent results on genetically modified CaM [48] in which the replacement of Glu residues 82-84 with three Lys residues resulted in a 70% reduction of the activation of myosin light-chain kinase.…”

Section: + -mentioning

confidence: 99%

Stimulation of the erythrocyte Ca²⁺‐ATPase and of bovine brain cyclic nucleotide phosphodiesterases by chemically modified calmodulin

Guerini¹,

Krebs²,

Carafoli³

1987

European Journal of Biochemistry

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Chemically modified calmodulins have been used to investigate structural features which are important for the interaction of the activator with targets. Carbamoylation of lysine residues had no influence on the ability of calmodulin to stimulate the plasma membrane CaZ +-ATPase whereas the stimulation of the bovine brain cyclicnucleotide phosphodiesterase was reduced up to 50%. Different species of carbamoylated calmodulin have been isolated but no differences were detected in their interaction with the cyclic-nucleotide phosphodiesterase. Modification of arginine residues by 1,2-~yclohexanedione had no effect on the stimulation of the phosphodiesterase but reduced by 40% the stimulation of the erythrocyte CaZ + ATPase. Mild oxidation of methionines by N-chlorsuccinimide produced a number of differently modified calmodulins. The different species have been purified and the modified residues have been identified. They affected the two different test enzymes to different extents indicating that methionines in the central helix of calmodulin are of greater importance for the interaction with the phosphodiesterase, whereas methionines located in the C-terminal half of calmodulin are more important for the interaction with the CaZ+-ATPase.Calmodulin (CaM) is the major modulator of the intracellular Ca2+ message [l, 21. It undergoes profound conformational changes upon binding of Ca2 + (see [3 -51 for recent reviews), resulting in the increase of the a-helical content [6] and in the exposure of hydrophobic sites [7]. The crystal structure of CaM in the Cazt-bound form [8] shows a dumb-bell-shaped molecule, with an eight-turn central a helix spanning residues 66 -92. Information on the structural aspects of the interaction of CaM with targets is still very scarce. The CaM-binding domain of myosin light-chain kinase from skeletal [9] and smooth muscle [lo, 111 has recently been isolated and sequenced. In analogy with the primary structure of CaM-binding peptides [12-141 it consists of clusters of basic amino acids and of stretches of hydrophobic residues, conferring to the domain amphipathic properties. It may be interesting to mention in this context that most anticalmodulin drugs are hydrophobic molecules containing positive charges [15, 161. It has been shown that the a-helical content of the CaM-binding domain of myosin light-chain kinase increases upon binding to CaM [9, 171. No structural information is available on the CaM-binding domain of the Ca2 +-pumping ATPase of plasma membranes, but recent work has indicated that its CaM-interacting region is a terminal sequence of approximately 9 kDa [18], consisting of a 4-kDa CaM-binding domain, and of a 5-kDa sequence which is essential for the expression of CaM stimulation [19]. Studies with proteolytic fragments of CaM have indicated that different regions of the molecule may be involved in its interaction with different targets [20, 211. In particular, the region encompassing the third Ca2+-binding loop (residues 91 -106) appears to play an important role in the i...

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Interaction of calmodulin and a calmodulin-binding peptide from myosin light chain kinase: major spectral changes in both occur as the result of complex formation

Cited by 134 publications

References 24 publications

A C-terminal, calmodulin-like regulatory domain from the plasma membrane Ca2+-pumping ATPase.

A C-terminal, calmodulin-like regulatory domain from the plasma membrane Ca2+-pumping ATPase.

Structures and related properties of helical, disulfide-stabilized peptides

Stimulation of the erythrocyte Ca²⁺‐ATPase and of bovine brain cyclic nucleotide phosphodiesterases by chemically modified calmodulin

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Interaction of calmodulin and a calmodulin-binding peptide from myosin light chain kinase: major spectral changes in both occur as the result of complex formation

Cited by 134 publications

References 24 publications

A C-terminal, calmodulin-like regulatory domain from the plasma membrane Ca2+-pumping ATPase.

A C-terminal, calmodulin-like regulatory domain from the plasma membrane Ca2+-pumping ATPase.

Structures and related properties of helical, disulfide-stabilized peptides

Stimulation of the erythrocyte Ca2+‐ATPase and of bovine brain cyclic nucleotide phosphodiesterases by chemically modified calmodulin

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Stimulation of the erythrocyte Ca²⁺‐ATPase and of bovine brain cyclic nucleotide phosphodiesterases by chemically modified calmodulin