The molecular anatomy of caldesmon

Marston, Steven B.; Redwood, Charles

doi:10.1042/bj2790001

Cited by 224 publications

(189 citation statements)

References 170 publications

(279 reference statements)

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“…(EEEKKAAEERAKA),S . present in caldesmon, is likely to be a helix [24]. Accordingly, we suspect that KEKEs form helices, and these, in turn, may form coiled-coils.…”

Section: [K 1 G a D X B X X X X X G X I X X E Jz]-(gqap)-n E K V V Nmentioning

confidence: 99%

KEKE motifs

1994

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A stretch of 28 'alternating' lysine (K) and glutamate (E) residues is found in an activator of the multicatalytic protease. Such 'KEKE sequences' are also present in subunits of the multicatalytic protease, in subunits of the 26s protease and in a variety of chaperonins. We propose that KEKE regions promote association between protein complexes. Furthermore, they may contribute to the selection of peptides presented on MHC Class I receptors.

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“…(EEEKKAAEERAKA),S . present in caldesmon, is likely to be a helix [24]. Accordingly, we suspect that KEKEs form helices, and these, in turn, may form coiled-coils.…”

Section: [K 1 G a D X B X X X X X G X I X X E Jz]-(gqap)-n E K V V Nmentioning

confidence: 99%

KEKE motifs

1994

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“…h-Caldesmon has since been found in all types of smooth muscle and a lower molecular weight variant of approximately 80,000 Da (I-caldesmon) has been identified in non-muscle cells [2,3]. Moreover, cDNA's fcr both forms have been cloned and sequenced [4,5].…”

Section: Introductionmentioning

confidence: 99%

Phosphorylation sequences in h‐caldesmon from phorbol ester‐stimulated canine aortas

1992

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The high molecular weight form of caldesmon (h‐caldesmon) is phosphorylated in vascular smooth muscle. The stoichiometry of caldesmon phosphorylation increases in response to stimulation of the muscle by several contractile agonists; however, the responsible kinase has not been identified. In this study, we have sequenced the phosphopeptides prepared from h‐caldesmon phosphorylated in vitro by protein kinase C (PKC) as well as the phosphopeptides prepared from caldesmon phosphorylated in intact canine aortas that were stimulated to contract with PDBu. PKC phosphorylated three sites located in the C terminus: GSS*LKIEE, AEFLNKS*VQK and NLWEKQS*VDK, while h‐caldesmon from intact tissue was phosphorylated at two separate sites also in the C terminus: VTS*PTKV and S*PAPK. By comparison to known substrate consensus sequences for various protein kinases these data suggest that h‐caldesmon is directly phosphorylated by a proline‐directed protein kinase and not by PKC.

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“…F-actin was not found in the pellet under these conditions but sediments when proteins cross-link filaments because of multiple actin-binding sites in a single polypeptide (20,28,29). As shown in Fig.…”

Section: Dfr-mlck Peptides Bind To Actinmentioning

confidence: 99%