Identification of a 52-kD calmodulin-binding protein associated with the mitotic spindle apparatus in mammalian cells.

Brady, Richard C.; Cabral, Fernando; Dedman, John R.

doi:10.1083/jcb.103.5.1855

Cited by 16 publications

(6 citation statements)

References 36 publications

(30 reference statements)

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“…This suggests that anaphase would not require a motor, but only controlled depolymerization at the plus end of microtubules of the kinetochor¢ fibers, consistent with a recently proposed model [28], More recent experimental results obtained with permeabilized cells models favor the idea that ATP would be required at anaphase for microtubule disassembly and not as a substrate for a motor exerting poleward forces on the chromosomes [84]. Other results have shown that calmodulin is associated with the mitotic spindle indirectly through binding to a calmodulin.binding protein [7], and that the free Ca 2+ concentration changes during mitosis [72]. Furthermore, mitosis has been shown to be inhibited, in sand dollar embryos, by microinjection of antiho-2+ dies directed against the muscle ~Ca pump [83].…”

Section: Mitosissupporting

confidence: 77%

From cilia and flagella to intracellular motility and back again: a review of a few aspects of microtubule‐based motility

Huitorel

1988

Biology of the Cell

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Ciliary or flagellar movement is the model of microtubule-dependent motility, the best studied at the molecular level. It is based on the relative sliding of outer doublets of microtubules that are linked at their proximal end to the basal structure and interconnected by associated proteins, among which dynein ATPase is at the origin of the movement. It is regulated from inside and outside media by various diffusible factors such as Ca2+, cyclic adenosine monophosphate (cAMP), polypeptides and so on (see other conferences presented during this meeting). Other motility processes are based on microtubules: vesicle and organelle transport through the cytoplasm (axonal flow in neurons, pigment granule movements in fish chromatophores, movements of particles along heliozoan axopods, etc.) could be mediated by microtubule motors such as kinesin or MAP 1C. Kinesin and MAP 1C, like dynein, are proteins that bind to microtubules and show an ATPase activity associated with force production. They differ from each other by their structure, and biochemical and pharmacological properties. The movements of chromosomes during mitosis and meiosis have long been studied, but are still poorly understood at the molecular level; this topic will be discussed in the light of recent data. Other constituents of the cytoskeleton are certainly involved in cellular motility: actin microfilaments and their motor myosin, intermediate filaments, non-actin filaments, all organized around the Microtubule Organizing Center (MTOC). As more information becomes available, it seems increasingly obvious that these various networks are closely interconnected and that each component probably modulates, resists, or favors properties of its partners, contributing to cellular and intracellular motility.

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Section: Mitosissupporting

confidence: 77%

From cilia and flagella to intracellular motility and back again: a review of a few aspects of microtubule‐based motility

Huitorel

1988

Biology of the Cell

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“…This difference was previously noted and reported in various mitotic cells (1,2,7,19,23,24), although the exogenous calmodulin can bind to tubulin (12,13) or to microtubules (4,5) in the mitotic apparatus. The accumulation of calmodulin in the polar regions of the spindle can be explained by the preferential binding of calmodulin to some calmodulin-binding proteins specifically localized in the polar regions of the spindle, as shown in mammalian cells (2).…”

Section: Discussionmentioning

confidence: 45%

A comparative study of the distribution of fluorescently labeled calmodulin and tubulin in the meiotic apparatus of the mouse oocyte.

Hamaguchi

Iwasa

Toriyama

et al. 1989

Cell Struct. Funct.

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ABSTRACT. The localizations of tubulin and calmodulin were investigated in the mouse oocyte during the second meiosis by fluorescently labeling and microinjecting these proteins prepared from porcine brain tissue. When injected, both tubulin and calmodulin were quickly incorporated into the preformed meiotic apparatus of the oocyte at metaphase. The localization of labeled tubulin was coincident with that of birefringence. However, the localization of labeled calmodulin was somewhat different: the fluorescence of calmodulin was intense in the polar regions of the spindle. After the chromosomes began to move, followed by parthenogenetic activation upon microinjection of a calcium buffer, these two fluorescent proteins, localized in the meiotic apparatus, moved to the interzonal region of the spindle during anaphase. At late anaphase and throughout telophase, calmodulin was excluded from the mid-bodylike structures in the interzonal region, whereas tubulin did accumulate in these structures. (21) is useful for studying the dynamic behavior of cytoskeletal proteins during cell division (see ref. 6 as a review). In particular, fluorescently labeled tubulin and calmodulin have been used extensively to study the dynamics of these proteins in the mitotic apparatus during mitosis (6-8, 19, 24). Fluorescent analog cytochemistryThe mouse unfertilized oocyte is a useful material for studying mitosis because it is transparent, stays at metaphase of the second meiosis for many hours after ovulation, and resumes mitosis upon artificial fertilization and parthenogenetic activation (11, 16-18, 20, 22). However, this material has not yet been utilized for studying the dynamics of the cytoskeleton in living cells.In this study, we investigated the localizations of tubulin and calmodulin in the mouse oocyte by means of microinjection of these labeled proteins to determine the similarities and differences in their intracellular localization during the second meiosis.

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“…That pp50 is a Ca2+/CaM binding MAP therefore suggests its involvement. It is noteworthy that a Ca2+/CaM binding protein with an apparent molecular mass similar to pp50's may also be an animal MAP that mediates CaM's association with mitotic spindle MTs (Brady et al, 1986).…”

Section: Localizations Of Tubulin Cam and Ef-1a In Plantsmentioning

confidence: 99%

A Calmodulin-Sensitive Interaction between Microtubules and a Higher Plant Homolog of Elongation Factor-1a

Durso¹,

Cyr²

1994

The Plant Cell

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The microtubules (MTs) of higher plant cells are organized into arrays with essential functions in plant cell growth and differentiation; however, molecular mechanisms underlying the organization and regulation of these arrays remain largely unknown. We have approached this problem using tubulin affinity chromatography to isolate carrot proteins that interact with MTs. From these proteins, a 50-kD polypeptide was selectively purified by exploiting its Ca(2+)-dependent binding to calmodulin (CaM). This polypeptide was identified as a homolog of elongation factor-1 alpha (EF-1 alpha)--a highly conserved and ubiquitous protein translation factor. The carrot EF-1 alpha homolog bundles MTs in vitro, and moreover, this bundling is modulated by the addition of Ca2+ and CaM together (Ca2+/CaM). A direct binding between the EF-1 alpha homolog and MTs was demonstrated, providing novel evidence for such an interaction. Based on these findings, and others discussed herein, we propose that an EF-1 alpha homolog mediates the lateral association of MTs in plant cells by a Ca2+/CaM-sensitive mechanism.

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Identification of a 52-kD calmodulin-binding protein associated with the mitotic spindle apparatus in mammalian cells.

Cited by 16 publications

References 36 publications

From cilia and flagella to intracellular motility and back again: a review of a few aspects of microtubule‐based motility

From cilia and flagella to intracellular motility and back again: a review of a few aspects of microtubule‐based motility

A comparative study of the distribution of fluorescently labeled calmodulin and tubulin in the meiotic apparatus of the mouse oocyte.

A Calmodulin-Sensitive Interaction between Microtubules and a Higher Plant Homolog of Elongation Factor-1a

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