A second isoform of chicken brush border myosin I contains a 29‐residue inserted sequence that binds calmodulin

Halsall, David; Hammer, John A.

doi:10.1016/0014-5793(90)80305-3

Cited by 49 publications

(23 citation statements)

References 17 publications

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“…All of these alternative splicings conserve the reading frame. For some unconventional myosins, isoforms differing in the number of IQ domains (29,30), in the internal sequence of their tail, or in their C termini (31) (32). Comparison with the described three-dimensional structure of a conventional myosin head (11,12) shows that the "short-headed" myosin VIIA isoform described here would have at least one The myosin VIIA gene was expressed in the otocyst and olfactory epithelium of 7-and 8-week-old human embryos ( Fig.…”

Section: Methodsmentioning

confidence: 70%

Human myosin VIIA responsible for the Usher 1B syndrome: a predicted membrane-associated motor protein expressed in developing sensory epithelia.

Weil

Lévy

Sahly

et al. 1996

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

166

147

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Section: Methodsmentioning

confidence: 70%

Human myosin VIIA responsible for the Usher 1B syndrome: a predicted membrane-associated motor protein expressed in developing sensory epithelia.

Weil

Lévy

Sahly

et al. 1996

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

166

147

View full text Add to dashboard Cite

“…These proteins all contain one or more copies ofa sequence, now called the IQ motif(5), consisting of a basic 23-aa unit including a common sequence of IQX3RGX3R (where X is any amino acid) shown to bind calmodulin (34,37,38). The bovine form of MMIP has three similar IQ motifs located in the "neck" region of the protein (aa 698-767).…”

Section: Resultsmentioning

confidence: 99%

Domain structure of a mammalian myosin I beta.

Reizes

Baryłko²,

et al. 1994

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

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We have determined the primary structure of a myosin I (called m myosin I, MMI3) from bovine brain and Identified Its functional domain. The protein was previously purified from brain and adrenal gand. Several constructs were generated and expressed in Escherichia cofl as glutathione S-traferase fusion proteins and the recombinant proteins were recognized by monoclona antibodies that recognize either "head" or "tail" dom of native myosin I. A gel overlay method was used to confirm that dulin binds to the consensus calmodulin-binding sequence in MMIIJ. Binding assays were used to detect interaction with anionic phospholipid vesicles. We conclude that MMI_3 consists of an amino-terminal 80.5-kDa domain that contains the ATP-and actin-binding sites, followed by an 8.5-kDa domain with three calmodulin-bindng sequences and a basic 30-kDa carboxylterminal tail segment that binds to anionic phospholipids and membranes.

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“…As shown in Fig. 7, the IQ motif, a consensus sequence in CaM-binding proteins (37), can be assigned to the latter peptide, although the matching was not complete.…”

mentioning

confidence: 98%

The Structure and Function of the Actin-binding Domain of Myosin Light Chain Kinase of Smooth Muscle

Ye¹,

Hayakawa²,

Kishi³

et al. 1997

Journal of Biological Chemistry

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In addition to its kinase activity, the myosin light chain kinase (MLCK) of smooth muscle has an actin binding activity through which it can regulate the actinmyosin interaction of smooth muscle (Kohama, K., Okagaki, T., Hayakawa, K., Lin, Y., Ishikawa, R., Shimmen In addition to this kinase activity, MLCK can act as an actin-binding protein; MLCK is present in association with the sarcomeric I-band (2), and it binds to actin filaments with a high affinity (3-5). We have shown that MLCK can inhibit the ATP-dependent interaction between actin and myosin by binding to actin filaments. This inhibition can be relieved by Ca 2ϩ /CaM, as was demonstrated by avoiding the complication derived from its kinase activity (6 -8), although the demonstration was limited to in vitro only.Such an inhibition, however, is not peculiar to MLCK. Caldesmon (see Ref. 9 for a review) and calponin (10) The relationship between the structure of MLCK and the function of the kinase activity in phosphorylating the myosin light chain and how Ca 2ϩ /CaM modulates the activity has been well established (see Ref. 13 for a review). However, there has been little study of the structure-function relationship of the actin binding activity except for the purification of an actinbinding fragment from MLCK (14).In this study, we have investigated which sequence of MLCK is responsible for the actin binding activity, which sequence inhibits the actin-myosin interaction, and which sequence binds CaM to relieve the inhibition. Our approach has been to cleave MLCK to prepare native fragments containing the actin binding activity (14), to design MLCK cDNA to express the recombinant fragments of actin binding activity in Escherichia coli, and then to analyze them biochemically. A few peptides have been synthesized to confirm these analyses. We have shown that: (i) MLCK has two actin-binding sites on the Nterminal side away from the central kinase domain, (ii) the binding site responsible for the inhibitory effect is at the Met MATERIALS AND METHODSPreparation of Proteins-All procedures were carried out at 0 -4°C. The purity of proteins was routinely monitored by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) (see below) so * This work was supported in part by grants from the Fujisawa Foundation and the Mitsubishi Foundation and by grants-in-aid for scientific research from the Ministry of Education, Science and Culture of Japan. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.ʈ To whom correspondence should be addressed. Tel.: 81-27-220-7960; Fax: 81-27-235-1401 or 81-27-220-7962. 1 The abbreviations used are: MLCK, myosin light chain kinase; CaM, calmodulin; PAGE, polyacrylamide gel electrophoresis; NTCB fragment, chicken gizzard MLCK fragment produced by the cleavage with 2-nitro-5-thiocyanatobenzoic acid; NN fragment, expressed fragment (amino acids 1-337 ...

show abstract

A second isoform of chicken brush border myosin I contains a 29‐residue inserted sequence that binds calmodulin

Cited by 49 publications

References 17 publications

Human myosin VIIA responsible for the Usher 1B syndrome: a predicted membrane-associated motor protein expressed in developing sensory epithelia.

Human myosin VIIA responsible for the Usher 1B syndrome: a predicted membrane-associated motor protein expressed in developing sensory epithelia.

Domain structure of a mammalian myosin I beta.

The Structure and Function of the Actin-binding Domain of Myosin Light Chain Kinase of Smooth Muscle

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