In ovo electroporation of <i>Crim1</i> in the developing chick spinal cord

Kolle, Gabriel; Jansen, A.H.M.; Yamada, Tomonori; Little, Melissa H.

doi:10.1002/dvdy.10204

Cited by 16 publications

(16 citation statements)

References 28 publications

(32 reference statements)

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“…crim1 was detected in the otic vesicle at and before 30 hpf ( (Lawson and Weinstein, 2002a), suggesting that crim1 may be present in angioblasts. Overall, expression of crim1 in zebrafish was consistent with previous reports in human, mouse and chicken revealing expression in several developmental tissues and organs including the notochord, otic vesicle and blood vessel precursors (Glienke et al, 2002;Kolle et al, 2000Kolle et al, , 2003.…”

Section: Expression Of Crim1 In Zebrafishsupporting

confidence: 92%

Knockdown of zebrafish crim1 results in a bent tail phenotype with defects in somite and vascular development

Kinna

Kolle

Carter

et al. 2006

Mechanisms of Development

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The Crim1 gene encodes a transmembrane protein containing six cysteine-rich repeats similar to those found in the BMP antagonist, chordin (chd). To investigate its physiological role, zebrafish crim1 was cloned and shown to be both maternally and zygotically expressed during zebrafish development in sites including the vasculature, intermediate cell mass, notochord, and otic vesicle. Bent or hooked tails with U-shaped somites were observed in 85% of morphants from 12 hpf. This was accompanied by a loss of muscle pioneer cells. While morpholino knockdown of crim1 showed some evidence of ventralisation, including expansion of the intermediate cell mass (ICM), reduction in head size bent tails and disruption to the somites and notochord, this did not mimic the classically ventralised phenotype, as assessed by the pattern of expression of the dorsal markers chordin, otx2 and the ventral markers eve1, pax2.1, tal1 and gata1 between 75% epiboly and six-somites. From 24 hpf, morphants displayed an expansion of the ventral mesoderm-derived ICM, as evidenced by expansion of tal1, lmo2 and crim1 itself. Analysis of the crim1 morphant phenotype in Tg(fli:EGFP) fish showed a clear reduction in the endothelial cells forming the intersegmental vessels and a loss of the dorsal longitudinal anastomotic vessel (DLAV). Hence, the primary role of zebrafish crim1 is likely to be the regulation of somitic and vascular development.

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Section: Expression Of Crim1 In Zebrafishsupporting

confidence: 92%

Knockdown of zebrafish crim1 results in a bent tail phenotype with defects in somite and vascular development

Kinna

Kolle

Carter

et al. 2006

Mechanisms of Development

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“…There is also an arginine/lysine-rich domain at the C-terminus. CG13253 shares homology with vertebrate Crim1 (Kolle et al, 2000;Kolle et al, 2003), which encodes a single-pass transmembrane protein with an N-terminal IGFBPlike domain, a short C-terminal cytoplasmic tail, and six CRRs interspersed between the IGFBP motif and the putative transmembrane domain (Kolle et al, 2000). Crim1 is expressed in early populations of motoneurons and interneurons in the developing mouse, although its neuronal function remains obscure (Wilkinson et al, 2003).…”

Section: Resultsmentioning

confidence: 99%

“…The presence of these two sequence elements renders Cmpy similar to vertebrate Crim1 (Kolle et al, 2000;Kolle et al, 2003). In mice, Crim1 hypomorphs have been described and display pleiotropic defects in multiple organ systems (Pennisi et al, 2007).…”

Section: Discussionmentioning

confidence: 99%

“…cmpy is predicted to encode a cysteine-rich repeat (CRR)-containing singlepass transmembrane protein, with sequence homology to vertebrate Cysteine-rich transmembrane BMP regulator 1 (Crim1) (Kolle et al, 2000;Kolle et al, 2003;Wilkinson et al, 2003). CRRs are present in a large number of BMP-interacting proteins in vertebrates and invertebrates (Umulis et al, 2009;Walsh et al, 2010).…”

Section: Introductionmentioning

confidence: 99%

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Crimpy inhibits the BMP homolog Gbb in motoneurons to enable proper growth control at theDrosophilaneuromuscular junction

James

Broihier

2011

Development

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SUMMARYThe BMP pathway is essential for scaling of the presynaptic motoneuron arbor to the postsynaptic muscle cell at the Drosophila neuromuscular junction (NMJ). Genetic analyses indicate that the muscle is the BMP-sending cell and the motoneuron is the BMPreceiving cell. Nevertheless, it is unclear how this directionality is established as Glass bottom boat (Gbb), the known BMP ligand, is active in motoneurons. We demonstrate that crimpy (cmpy) limits neuronal Gbb activity to permit appropriate regulation of NMJ growth. cmpy was identified in a screen for motoneuron-expressed genes and encodes a single-pass transmembrane protein with sequence homology to vertebrate Cysteine-rich transmembrane BMP regulator 1 (Crim1). We generated a targeted deletion of the cmpy locus and find that loss-of-function mutants exhibit excessive NMJ growth. In accordance with its expression profile, tissue-specific rescue experiments indicate that cmpy functions neuronally. The overgrowth in cmpy mutants depends on the activity of the BMP type II receptor Wishful thinking, arguing that Cmpy acts in the BMP pathway upstream of receptor activation and raising the possibility that it inhibits Gbb activity in motoneurons. Indeed, the cmpy mutant phenotype is strongly suppressed by RNAi-mediated knockdown of Gbb in motoneurons. Furthermore, Cmpy physically interacts with the Gbb precursor protein, arguing that Cmpy binds Gbb prior to the secretion of mature ligand. These studies demonstrate that Cmpy restrains Gbb activity in motoneurons. We present a model whereby this inhibition permits the muscle-derived Gbb pool to predominate at the NMJ, thus establishing the retrograde directionality of the pro-growth BMP pathway.

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“…Cmpy was identified in a screen for motoneuron-expressed genes and codes for a single-pass transmembrane protein that physically interacts with Gbb. It has sequence homology to the vertebrate transmembrane BMP-binding protein Crim1 (Cysteine-rich in motoneurons-1) (Kolle et al, 2000; Kolle et al, 2003). Loss of Cmpy results in NMJ overgrowth, which is rescued by knockdown of Gbb in motoneurons.…”

Section: Introductionmentioning

confidence: 99%

Crimpy Enables Discrimination of Presynaptic and Postsynaptic Pools of a BMP at the Drosophila Neuromuscular Junction

et al. 2014

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Summary Distinct pools of the BMP Glass bottom boat (Gbb) control structure and function of the Drosophila neuromuscular junction. Specifically, motoneuron-derived Gbb regulates baseline neurotransmitter release, while muscle-derived Gbb regulates NMJ growth. Yet how cells differentiate between these ligand pools is not known. Here we present evidence that the neuronal Gbb-binding protein Crimpy (Cmpy) permits discrimination of pre and postsynaptic ligand by serving sequential functions in Gbb signaling. Cmpy first delivers Gbb to dense core vesicles (DCVs) for activity-dependent release from presynaptic terminals. In the absence of Cmpy, Gbb is no longer associated with DCVs and is not released by activity. Electrophysiological analyses demonstrate that Cmpy promotes Gbb's pro-neurotransmission function. Surprisingly, the Cmpy ectodomain is itself released upon DCV exocytosis, arguing that Cmpy serves a second function in BMP signaling. In addition to trafficking Gbb to DCVs, we propose that Gbb/Cmpy co-release from presynaptic terminals defines a neuronal pro-transmission signal.

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In ovo electroporation of Crim1 in the developing chick spinal cord

Cited by 16 publications

References 28 publications

Knockdown of zebrafish crim1 results in a bent tail phenotype with defects in somite and vascular development

Knockdown of zebrafish crim1 results in a bent tail phenotype with defects in somite and vascular development

Crimpy inhibits the BMP homolog Gbb in motoneurons to enable proper growth control at theDrosophilaneuromuscular junction

Crimpy Enables Discrimination of Presynaptic and Postsynaptic Pools of a BMP at the Drosophila Neuromuscular Junction

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