Purification of microtubule proteins from <i>Xenopus</i> egg extracts: Identification of a 230K MAP4‐like protein

Faruki, Shamsa; Karsenti, Eric

doi:10.1002/cm.970280203

Cited by 22 publications

(10 citation statements)

References 34 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…MAP4 was considered a likely candidate, as well as other related ones (e.g. XMAP from Xenopus eggs, Faruki and Karsenti (1994)). Regarding kinases, cdc2 and MAP kinases were suggested as potential triggers of microtubule reorganization (Gotoh et al, 1991;Verde et al, 1992;Lieuvin et al, 1994;Ookata et al, 1995).…”

Section: Discussionmentioning

confidence: 99%

Phosphorylation of Microtubule-associated Proteins MAP2 and MAP4 by the Protein Kinase p110mark

Illenberger

Drewes

Trinczek

et al. 1996

Journal of Biological Chemistry

186

173

View full text Add to dashboard Cite

Section: Discussionmentioning

confidence: 99%

Phosphorylation of Microtubule-associated Proteins MAP2 and MAP4 by the Protein Kinase p110mark

Illenberger

Drewes

Trinczek

et al. 1996

Journal of Biological Chemistry

186

173

View full text Add to dashboard Cite

“…Scale bars are 25 µm in A and 10 µm in B. 1994; Faruki and Karsenti, 1994;Gard and Kirschner,1987b;Jessus et al, 1985;Shiina et al, 1992). Results from in vitro studies have shown that XMAP230 (Anderson et al, 1994) and XMAP310 Anderson and Karsenti, 1997) stabilize MTs and suppress dynamic instability in vitro, similar to the effects of MAPs isolated from vertebrate brain (Drechsel et al, 1992;Pryer et al, 1992).…”

Section: Regulation Of Mt Assembly and Organizationmentioning

confidence: 90%

Confocal microscopy and 3‐D reconstruction of the cytoskeleton of Xenopus oocytes

Gard¹

1999

Microsc. Res. Tech.

View full text Add to dashboard Cite

Xenopus oocytes contain a complex cytoskeleton composed of three filament systems: (1) microtubules, composed of tubulin and at least three different microtubule-associated proteins (XMAPs); (2) microfilaments composed of actin and associated proteins; and (3) intermediate filaments, composed of keratins. For the past several years, we have used confocal immunofluorescence microscopy to characterize the organization of the oocyte cytoskeleton throughout the course of oogenesis. Together with computer-assisted reconstruction of the oocyte in three dimensions, confocal microscopy gives an unprecedented view of the assembly and reorganization of the cytoskeleton during oocyte growth and differentiation. Results of these studies, combined with the effects of cytoskeletal inhibitors, suggest that organization of the cytoskeleton in Xenopus oocytes is dependent upon a hierarchy of interactions between microtubules, microfilaments, and keratin filaments. This article presents a gallery of confocal images and 3-D reconstructions depicting the assembly and organization of the oocyte cytoskeleton during stages 0-VI of oogenesis, a discussion of the mechanisms that might regulate cytoskeletal organization during oogenesis, and speculates on the potential roles of the oocyte cytoskeleton during oogenesis and axis formation.

show abstract

“…MAPs are good substrates for many protein kinases in vitro [21], and their phosphorylation was shown to reduce the ability of MTs to polymerize in vitro [22]. MAPs include tau and MAP2, which are expressed abundantly only in nervous tissue, and MAP4, expressed ubiquitously in non-neuronal cells [23]. The phosphorylation state of MAP4 is thought to be a key factor in the regulation of MT stability.…”

Section: Introductionmentioning

confidence: 99%

The p38/MAPK pathway regulates microtubule polymerization through phosphorylation of MAP4 and Op18 in hypoxic cells

Chu

Han

et al. 2009

Cell. Mol. Life Sci.

111

View full text Add to dashboard Cite

In both cardiomyocytes and HeLa cells, hypoxia (1% O(2)) quickly leads to microtubule disruption, but little is known about how microtubule dynamics change during the early stages of hypoxia. We demonstrate that microtubule associated protein 4 (MAP4) phosphorylation increases while oncoprotein 18/stathmin (Op18) phosphorylation decreases after hypoxia, but their protein levels do not change. p38/MAPK activity increases quickly after hypoxia concomitant with MAP4 phosphorylation, and the activated p38/MAPK signaling leads to MAP4 phosphorylation and to Op18 dephosphorylation, both of which induce microtubule disruption. We confirmed the interaction between phospho-p38 and MAP4 using immunoprecipitation and found that SB203580, a p38/MAPK inhibitor, increases and MKK6(Glu) overexpression decreases hypoxic cell viability. Our results demonstrate that hypoxia induces microtubule depolymerization and decreased cell viability via the activation of the p38/MAPK signaling pathway and changes the phosphorylation levels of its downstream effectors, MAP4 and Op18.

show abstract

Purification of microtubule proteins from Xenopus egg extracts: Identification of a 230K MAP4‐like protein

Cited by 22 publications

References 34 publications

Phosphorylation of Microtubule-associated Proteins MAP2 and MAP4 by the Protein Kinase p110mark

Phosphorylation of Microtubule-associated Proteins MAP2 and MAP4 by the Protein Kinase p110mark

Confocal microscopy and 3‐D reconstruction of the cytoskeleton of Xenopus oocytes

The p38/MAPK pathway regulates microtubule polymerization through phosphorylation of MAP4 and Op18 in hypoxic cells

Contact Info

Product

Resources

About