A leucine‐rich repeat peptide derived from the <i>Drosophila</i> Toll receptor forms extended filaments with a β‐sheet structure

Gay, Nicholas J.; Packman, Leonard C.; Weldon, Michael A.; Barna, Jennifer C. J.

doi:10.1016/0014-5793(91)81110-t

Cited by 71 publications

(44 citation statements)

References 19 publications

(9 reference statements)

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“…The LRR domain of yeast Rna1p has a crescent or horseshoe shape with an interior parallel b-sheet and an exterior array of a-helices (Hillig et al, 1999;Rose and Meier, 2001). This type of structure is often involved in the formation of protein-protein interactions (Gay et al, 1991;Kobe and Deisenhofer, 1995;Kobe and Kajava, 2001). Unlike other activating proteins of small GTPases, RanGAP does not act through an arginine finger (Seewald et al, 2002).…”

Section: Lrr Domain Loop Region Amino Acids Contribute To Gap Activitmentioning

confidence: 99%

GAP Activity, but Not Subcellular Targeting, Is Required for Arabidopsis RanGAP Cellular and Developmental Functions

et al. 2015

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The Ran GTPase activating protein (RanGAP) is important to Ran signaling involved in nucleocytoplasmic transport, spindle organization, and postmitotic nuclear assembly. Unlike vertebrate and yeast RanGAP, plant RanGAP has an N-terminal WPP domain, required for nuclear envelope association and several mitotic locations of Arabidopsis thaliana RanGAP1. A double null mutant of the two Arabidopsis RanGAP homologs is gametophyte lethal. Here, we created a series of mutants with various reductions in RanGAP levels by combining a RanGAP1 null allele with different RanGAP2 alleles. As RanGAP level decreases, the severity of developmental phenotypes increases, but nuclear import is unaffected. To dissect whether the GAP activity and/or the subcellular localization of RanGAP are responsible for the observed phenotypes, this series of rangap mutants were transformed with RanGAP1 variants carrying point mutations abolishing the GAP activity and/or the WPPdependent subcellular localization. The data show that plant development is differentially affected by RanGAP mutant allele combinations of increasing severity and requires the GAP activity of RanGAP, while the subcellular positioning of RanGAP is dispensable. In addition, our results indicate that nucleocytoplasmic trafficking can tolerate both partial depletion of RanGAP and delocalization of RanGAP from the nuclear envelope.

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Section: Lrr Domain Loop Region Amino Acids Contribute To Gap Activitmentioning

confidence: 99%

GAP Activity, but Not Subcellular Targeting, Is Required for Arabidopsis RanGAP Cellular and Developmental Functions

et al. 2015

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“…The latter includes, for example, the polyglutamine-containing proteins responsible for Huntington's disease (Stott et al, 1995), the leucinerich repeat peptide of the Drosophila Toll protein (Gay et al, 1991), and the amyloid fibres linked to Alzheimer's disease (Kelly, 1996) and transmissible spongiform encephalopathies (Aguzzi & Weissmann, 1997;Harrison et al, 1997). Finally, the possibility of intermediate formation of a-helices in the folding of p-sheetcontaining proteins attracts interest in a to p transitions also with regard to rational protein design (Carey, 1996).…”

Section: T Szyperski Et Almentioning

confidence: 99%

Pulmonary surfactant‐associated polypeptide C in a mixed organic solvent transforms from a monomeric α‐helical state into insoluble β‐sheet aggregates

Szyperski¹,

Vandenbussche²,

Curstedt

et al. 1998

Protein Science

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In the 35-residue pulmonary surfactant-associated lipopolypeptide C (SP-C), the stability of the valyl-rich tu-helix comprising residues 9-34 has been monitored by circular dichroism, nuclear magnetic resonance, and Fourier transform infrared spectroscopy in both a mixed organic solvent and in phospholipid micelles. The a-helical form of SP-C observed in freshly prepared solutions in a mixed solvent of CHC13/CH30H/O.I M HCI 32:64:undergoes within a few days an irreversible transformation to an insoluble aggregate that contains P-sheet secondary structure. Hydrogen exchange experiments revealed that this conformational transition proceeds through a transition state with an Eyring free activation enthalpy of about 100 kJ mol", in which the polypeptide segment 9-27 largely retains a helical conformation. In dodecylphosphocholine micelles, the helical form of SP-C was maintained after seven weeks at 50°C. The a-helical form of SP-C thus seems to be the thermodynamically most stable state in this micellar environment, whereas its presence in freshly prepared samples in the aforementioned mixed solvent is due to a high kinetic bamer for unfolding. These observations support a previously proposed pathway for in vivo synthesis of SP-C through proteolytic processing from a 21-kDa precursor protein.

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“…Four leucine-rich repeats (LRRs) comprise most of the protein. This motif is found in matrix proteins that bind to collagen or laminin (Matsushima et al, 2000), in transmembrane receptors, and in cell surface adhesion molecules (Gay et al, 1991;Nose et al, 1992;Yamagata et al, 1994). LRRs are thought to be required for protein recognition and adhesion events (Hocking et al, 1998).…”

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confidence: 99%

Repellent Signaling by Slit Requires the Leucine-Rich Repeats

et al. 2001

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Slit is a repellent axon guidance cue produced by the midline glia in Drosophila that is required to regulate the formation of contralateral projections and the lateral position of longitudinal tracts. Four sequence motifs comprise the structure of Slit: a leucine-rich repeat (LRR), epidermal growth factor-like (EGF) repeats, a laminin-like globular (G)-domain, and a cysteine domain. Here we demonstrate that the LRR is required for repellent signaling and in vitro binding to Robo. Repellent signaling by slit is reduced by point mutations that encode single amino acid changes in the LRR domain. By contrast to the EGF or G-domains, the LRR domain is required in transgenes to affect axon guidance. Finally, we show that the midline repellent receptor, Robo, binds Slit proteins with internal deletions that also retain repellent activity. However, Robo does not bind Slit protein missing the LRR. Taken together, our data demonstrate that Robo binding and repellent signaling by Slit require the LRR region.

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A leucine‐rich repeat peptide derived from the Drosophila Toll receptor forms extended filaments with a β‐sheet structure

Cited by 71 publications

References 19 publications

GAP Activity, but Not Subcellular Targeting, Is Required for Arabidopsis RanGAP Cellular and Developmental Functions

GAP Activity, but Not Subcellular Targeting, Is Required for Arabidopsis RanGAP Cellular and Developmental Functions

Pulmonary surfactant‐associated polypeptide C in a mixed organic solvent transforms from a monomeric α‐helical state into insoluble β‐sheet aggregates

Repellent Signaling by Slit Requires the Leucine-Rich Repeats

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