Xenopus interphase and mitotic microtubule-associated proteins differentially suppress microtubule dynamics in vitro

Andersen, Søren

doi:10.1002/(sici)1097-0169(1998)41:3<202::aid-cm2>3.0.co;2-x

Cited by 25 publications

(7 citation statements)

References 91 publications

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“…We know from previous studies that MAPs show a phosphorylation-dependent decrease in MT affinity during mitosis (ref. 21 and references therein). Moreover, it has been shown that mitotic MAPs promote MT assembly twofold less than interphase MAPs; purified phosphorylated MAPs are also known to promote MT assembly less than the corresponding unphosphorylated MAPs (ref.…”

Section: Microtubule-associated Proteins As Regulators Of Microtubule Dynamicsmentioning

confidence: 99%

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Balanced regulation of microtubule dynamics during the cell cycle: a contemporary view

Andersen

1999

Bioessays

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Assembly of mitotic and meiotic spindles into an elliptical bipolar shape is an example of morphogenetic processes that involve local chromosomal regulation of microtubule dynamics for proper spatial microtubule assembly. Global microtubule dynamics during the cell cycle and local microtubule dynamics during spindle assembly are regulated by a balance between microtubule stabilizing and destabilizing factors. How a chromosome‐induced phosphorylation gradient may be generated and modulate spindle microtubule assembly through balanced regulation of the activity of microtubule‐associated proteins and Stathmin/Op18 is analyzed. BioEssays 1999;21:53–60. © 1999 John Wiley & Sons, Inc.

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Section: Microtubule-associated Proteins As Regulators Of Microtubule Dynamicsmentioning

confidence: 99%

“…(29,43) well as their regulatory enzymes. (2,6,(21)(22)(23)63,64) We can therefore approach the proposed model (42,57) with greater molecular detail.…”

Section: How Do Chromosomes Promote Microtubule Assembly?mentioning

confidence: 99%

Balanced regulation of microtubule dynamics during the cell cycle: a contemporary view

Andersen

1999

Bioessays

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“…Two prime animal MAP families that bind tubulin and are recruited to microtubule plus ends by EB proteins (either directly or indirectly) are the Cytoplasmic Linker-Associated Protein (CLASP) family and the XMAP215 family of microtubule polymerases [16–20]. Both CLASP and XMAP215 members are critical for proper interphase microtubule dynamics as well as mitotic spindle structure and dynamics [16,21–23]. While XMAP215 family members promote microtubule polymerization, CLASP family members promote microtubule pause, potentiate rescue, and limit catastrophe [16,24–29].…”

Section: Introductionmentioning

confidence: 99%

Structures of TOG1 and TOG2 from the human microtubule dynamics regulator CLASP1

Leano

Slep

2019

PLoS ONE

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Tubulin-binding TOG domains are found arrayed in a number of proteins that regulate microtubule dynamics. While much is known about the structure and function of TOG domains from the XMAP215 microtubule polymerase family, less in known about the TOG domain array found in animal CLASP family members. The animal CLASP TOG array promotes microtubule pause, potentiates rescue, and limits catastrophe. How structurally distinct the TOG domains of animal CLASP are from one another, from XMAP215 family TOG domains, and whether a specific order of structurally distinct TOG domains in the TOG array is conserved across animal CLASP family members is poorly understood. We present the x-ray crystal structures of Homo sapiens ( H . s .) CLASP1 TOG1 and TOG2. The structures of H . s . CLASP1 TOG1 and TOG2 are distinct from each other and from the previously determined structure of Mus musculus ( M . m .) CLASP2 TOG3. Comparative analyses of CLASP family TOG domain structures determined to date across species and paralogs supports a conserved CLASP TOG array paradigm in which structurally distinct TOG domains are arrayed in a specific order. H . s . CLASP1 TOG1 bears structural similarity to the free-tubulin binding TOG domains of the XMAP215 family but lacks many of the key tubulin-binding determinants found in XMAP215 family TOG domains. This aligns with studies that report that animal CLASP family TOG1 domains cannot bind free tubulin or microtubules. In contrast, animal CLASP family TOG2 and TOG3 domains have reported microtubule-binding activity but are structurally distinct from the free-tubulin binding TOG domains of the XMAP215 family. H . s . CLASP1 TOG2 has a convex architecture, predicted to engage a hyper-curved tubulin state that may underlie its ability to limit microtubule catastrophe and promote rescue. M . m . CLASP2 TOG3 has unique structural elements in the C-terminal half of its α-solenoid domain that our modeling studies implicate in binding to laterally-associated tubulin subunits in the microtubule lattice in a mode similar to, yet distinct from those predicted for the XMAP215 family TOG4 domain. The potential ability of the animal CLASP family TOG3 domain to engage lateral tubulin subunits may underlie the microtubule rescue activity ascribed to the domain. These findings highlight the structural diversity of TOG domains within the CLASP family TOG array and provide a molecular foundation for understanding CLASP-dependent effects on microtubule dynamics.

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“…Microtubules and their associated proteins (MAPs) play a key role in a dynamic network that involves the regulation of cell shape and cell polarity during differentiation, chromosome partitioning at mitosis, and intracellular transport (Maccioni and Cambiazo 1995; Drewes et al 1998; Ebneth et al 1999; Marx et al 2000; Manabe et al 2002; Drewes 2004). During these processes, the binding of tau and MAPs to microtubules is controlled by their phosphorylation state, which is meditated by microtubule‐associated protein/microtubule affinity‐regulating kinases (MARKs) (Mercken et al 1995; Sato‐Harada et al 1996; Illenberger et al 1996; Andersen 1998; Drewes et al 1998; Li et al 2003; Trinczek et al 2004).…”

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confidence: 99%

Solution structure of the kinase‐associated domain 1 of mouse microtubule‐associated protein/microtubule affinity‐regulating kinase 3

et al. 2006

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Microtubule-associated protein/microtubule affinity-regulating kinases (MARKs)/PAR-1 are common regulators of cell polarity that are conserved from nematode to human. All of these kinases have a highly conserved C-terminal domain, which is termed the kinase-associated domain 1 (KA1), although its function is unknown. In this study, we determined the solution structure of the KA1 domain of mouse MARK3 by NMR spectroscopy. We found that approximately 50 additional residues preceding the previously defined KA1 domain are required for its proper folding. The newly defined KA1 domain adopts a compact alpha+beta structure with a betaalphabetabetabetabetaalpha topology. We also found a characteristic hydrophobic, concave surface surrounded by positively charged residues. This concave surface includes the highly conserved Glu-Leu-Lys-Leu motif at the C terminus, indicating that it is important for the function of the KA1 domain.

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Xenopus interphase and mitotic microtubule-associated proteins differentially suppress microtubule dynamics in vitro

Cited by 25 publications

References 91 publications

Balanced regulation of microtubule dynamics during the cell cycle: a contemporary view

Balanced regulation of microtubule dynamics during the cell cycle: a contemporary view

Structures of TOG1 and TOG2 from the human microtubule dynamics regulator CLASP1

Solution structure of the kinase‐associated domain 1 of mouse microtubule‐associated protein/microtubule affinity‐regulating kinase 3

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