The light chain composition of chicken brain myosin-Va: Calmodulin, myosin-II essential light chains, and 8-kDa dynein light chain/PIN

Espindola, Foued Salmen; Suter, Daniel M.; Partata, Leticia B.E.; Cao, Tracy T.; Wolenski, Joseph S.; Cheney, Richard E.; King, Stephen M.; Mooseker, Mark S.

doi:10.1002/1097-0169(200012)47:4<269::aid-cm2>3.0.co;2-g

Cited by 161 publications

(76 citation statements)

References 64 publications

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“…These LC8 binding partners include neuronal nitric oxide synthase (nNOS), 12 inhibitor of NF-κB transcription factor (IκBα), 13 the proapoptotic Bcl2 family protein Bim, 14 p53 binding protein 1, 15 neuronal scaffold GKAP, 16 transcriptional repressor 1 (TRPS1), 17 estrogen receptor, 18 and mitogen-activated protein kinase p38. 19 LC8 is also an integral component of the actin-based motor myosin V. 20,21 Most of these putative binding partners have either a KXTQTX or an XGIQVD sequence that have been recognized as LC8-binding motifs. 22 Several LC8 binding partners were initially identified by yeast two-hybrid analysis and the specificity of their interaction was subsequently verified either by glutathione-S-transferase pulldown studies of deletion mutants or by NMR on peptide fragments.…”

Section: Introductionmentioning

confidence: 99%

Structure and Dynamics of LC8 Complexes with KXTQT-Motif Peptides: Swallow and Dynein Intermediate Chain Compete for a Common Site

Benison

Karplus

Barbar

2007

Journal of Molecular Biology

109

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Section: Introductionmentioning

confidence: 99%

Structure and Dynamics of LC8 Complexes with KXTQT-Motif Peptides: Swallow and Dynein Intermediate Chain Compete for a Common Site

Benison

Karplus

Barbar

2007

Journal of Molecular Biology

109

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“…CaM has four high-affinity calciumbinding sites called EF-hands, each composed of two a-helices connected by a calcium-binding loop. Murine myosin Va isolated from tissue only binds CaM [11], while that isolated from chicken brain contains both CaM and a specific light chain of the essential light chain family (called L17 or L23) [12][13][14]. Based on analysis of proteolytic fragments of myoVa purified from chick brain, it was concluded that the specific light chain does not bind to IQ motif one or two [14].…”

Section: Lever Armmentioning

confidence: 99%

“…This was the first example showing that alternative exon usage in the rod can help specify particular cargoes, in addition to binding sites for cargo in the globular tail. The brain-specific exon B contains only three amino acids (DDK), but is essential for binding an~10-kDa light chain in the dynein family called DYNLL2 [39,40], which copurifies with myoVa isolated from chick brain [13]. Spectroscopic studies showed that binding of DYNLL2 increases the a-helical coiled-coil content in the region around its binding site.…”

Section: Rod Regionmentioning

confidence: 99%

Myosin V from head to tail

Trybus

2008

Cell. Mol. Life Sci.

165

139

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Myosin V (myoV), a processive cargo transporter, has arguably been the most well-studied unconventional myosin of the past decade. Considerable structural information is available for the motor domain, the IQ motifs with bound calmodulin or light chains, and the cargo-binding globular tail, all of which have been crystallized. The repertoire of adapter proteins that link myoV to a particular cargo is becoming better understood, enabling cellular transport processes to be dissected. MyoV is processive, meaning that it takes many steps on actin filaments without dissociating. Its extended lever arm results in long 36-nm steps, making it ideal for single molecule studies of processive movement. In addition, electron microscopy revealed the structure of the inactive, folded conformation of myoV when it is not transporting cargo. This review provides a background on myoV, and highlights recent discoveries that show why myoV will continue to be an active focus of investigation.

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“…Samples containing 25 μg total protein from each tissue homogenate were loaded onto gels, except for pituitary (15 μg) and pineal (not quantified). Myosin-Va, purified from 2-to 3-day-old chick brain, as described in Espindola et al (2000), were run on the same gels as a marker for the myosin Va heavy chain. As molecular weight markers, we used SDS-6H (Sigma-Aldrich, USA).…”

Section: Sds-polyacrylamide Gel Electrophoresis and Immunoblottingmentioning

confidence: 99%

Localization of myosin-Va in subpopulations of cells in rat endocrine organs

et al. 2008

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Myosin-Va is a Ca(2+)/calmodulin-regulated unconventional myosin involved in the transport of vesicles, membranous organelles, and macromolecular complexes composed of proteins and mRNA. The cellular localization of myosin-Va has been described in great detail in several vertebrate cell types, including neurons, melanocytes, lymphocytes, auditory tissues, and a number of cultured cells. Here, we provide an immunohistochemical view of the tissue distribution of myosin-Va in the major endocrine organs. Myosin-Va is highly expressed in the pineal and pituitary glands and in specific cell populations of other endocrine glands, especially the parafollicular cells of the thyroid, the principal cells of the parathyroid, the islets of Langerhans of the pancreas, the chromaffin cells of the adrenal medulla, and a subpopulation of interstitial testicular cells. Weak to moderate staining has been detected in steroidogenic cells of the adrenal cortex, ovary, and Leydig cells. Myosin-Va has also been localized to non-endocrine cells, such as the germ cells of the seminiferous epithelium and maturing oocytes and in the intercalated ducts of the exocrine pancreas. These data provide the first systematic description of myosin-Va localization in the major endocrine organs of rat.

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The light chain composition of chicken brain myosin-Va: Calmodulin, myosin-II essential light chains, and 8-kDa dynein light chain/PIN

Cited by 161 publications

References 64 publications

Structure and Dynamics of LC8 Complexes with KXTQT-Motif Peptides: Swallow and Dynein Intermediate Chain Compete for a Common Site

Structure and Dynamics of LC8 Complexes with KXTQT-Motif Peptides: Swallow and Dynein Intermediate Chain Compete for a Common Site

Myosin V from head to tail

Localization of myosin-Va in subpopulations of cells in rat endocrine organs

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