Differential expression of CPD1 during postnatal development in the mouse cerebellum

Radrizzani, Martı́n; Vilá-Ortíz, Guillermo J.; Cafferata, Eduardo G.; Tella, Marı́a Clara Di; Gonzalez-Guerrico, Anatilde; Perandones, Claudia; Pivetta, Omar H.; Carminatti, Héctor; Vargas, Victor P. Idoyaga; Santa‐Coloma, Tomás A.

doi:10.1016/s0006-8993(01)02351-4

Cited by 26 publications

(42 citation statements)

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“…Anp32e, also known as CPD1 ( c erebellum p ostnatal d evelopment gene 1), was first cloned due to its high expression in the postnatal mouse cerebellum 27 . In some reports, Anp32e has been referred to as LANPL ( l eucine-rich a cidic n uclear p rotein- l ike) because of its sequence homology with Anp32a (also known as LANP) 28 .…”

Section: Resultsmentioning

confidence: 99%

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Anp32e, a higher eukaryotic histone chaperone directs preferential recognition for H2A.Z

et al. 2014

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H2A.Z is a highly conserved histone variant in all species. The chromatin deposition of H2A.Z is specifically catalyzed by the yeast chromatin remodeling complex SWR1 and its mammalian counterpart SRCAP. However, the mechanism by which H2A.Z is preferentially recognized by non-histone proteins remains elusive. Here we identified Anp32e, a novel higher eukaryote-specific histone chaperone for H2A.Z. Anp32e preferentially associates with H2A.Z-H2B dimers rather than H2A-H2B dimers in vitro and in vivo and dissociates non-nucleosomal aggregates formed by DNA and H2A-H2B. We determined the crystal structure of the Anp32e chaperone domain (186-232) in complex with the H2A.Z-H2B dimer. In this structure, the region containing Anp32e residues 214-224, which is absent in other Anp32 family proteins, specifically interacts with the extended H2A.Z αC helix, which exhibits an unexpected conformational change. Genome-wide profiling of Anp32e revealed a remarkable co-occupancy between Anp32e and H2A.Z. Cells overexpressing Anp32e displayed a strong global H2A.Z loss at the +1 nucleosomes, whereas cells depleted of Anp32e displayed a moderate global H2A.Z increase at the +1 nucleosomes. This suggests that Anp32e may help to resolve the non-nucleosomal H2A.Z aggregates and also facilitate the removal of H2A.Z at the +1 nucleosomes, and the latter may help RNA polymerase II to pass the first nucleosomal barrier.

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Section: Resultsmentioning

confidence: 99%

“…It has been proposed that Anp32 family proteins functionally overlap and that the LRR domain is of particular importance 27 . Instead, Anp32 C-terminal regions, which are enriched with acidic residues and are more diverse in sequence, lack obvious function.…”

Section: Discussionmentioning

confidence: 99%

Anp32e, a higher eukaryotic histone chaperone directs preferential recognition for H2A.Z

et al. 2014

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“…LANP (mouse LANP: 247 amino acids; NCBI Reference Sequence: NP_033802.2) was the first to be discovered, identified on the basis of a proteomic screen for developmentally regulated proteins in the rat brain peaking in the first few weeks of life [6]. CPD1 (260 amino acids; NCBI Reference Sequence: NP_075699.3) was subsequently discovered using similar high-throughput methods; although in this case the technique of differential display was used to identify messenger RNAs that increase in the immediate postnatal period [7].…”

Section: Introductionmentioning

confidence: 99%

Cpd-1 Null Mice Display a Subtle Neurological Phenotype

2010

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BackgroundCPD1 (also known as ANP32-E) belongs to a family of evolutionarily conserved acidic proteins with leucine rich repeats implicated in a variety of cellular processes regulating gene expression, vesicular trafficking, intracellular signaling and apoptosis. Because of its spatiotemporal expression pattern, CPD1 has been proposed to play an important role in brain morphogenesis and synaptic development.Methodology/Principal FindingsWe have generated CPD1 knock-out mice that we have subsequently characterized. These mice are viable and fertile. However, they display a subtle neurological clasping phenotype and mild motor deficits.Conclusions/SignificanceCPD1 is not essential for normal development; however, it appears to play a role in the regulation of fine motor functions. The minimal phenotype suggests compensatory biological mechanisms.

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“…Thus APRIL, an acronym derived from A protein rich in leucines, is also known as PAL-31, for proliferation-associated leucine-rich protein, MW 31kDa, and SSP-29, for silver-stainable protein with a molecular mass of 29 kDa (24,25,41). CPD1 (cerebellar postnatal development protein 1), another LANP family member, has been called LANP-like protein (LANP-L) (21,28). Two human homologues of LANP/pp32 have been called pp32r1 and pp32r2 to signify that they are related (14,15).…”

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Generation and Characterization of LANP/pp32 Null Mice

Opal

Garcı́a

McCall

et al. 2004

Molecular and Cellular Biology

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The leucine-rich acidic nuclear protein (LANP) belongs to a family of evolutionarily conserved proteins that are characterized by an amino-terminal domain rich in leucine residues followed by a carboxy-terminal acidic tail. LANP has been implicated in the regulation of a variety of cellular processes including RNA transport, transcription, apoptosis, vesicular trafficking, and intracellular signaling. Abundantly expressed in the developing cerebellum, this protein has also been hypothesized to play a role in cerebellar morphogenesis. LANP has been implicated in disease biology as well, both as a mediator of toxicity in spinocerebellar ataxia type 1 and as a tumor suppressor in cancers of the breast and prostate. To better understand the function of this multifaceted protein, we have generated mice lacking LANP. Surprisingly, these mice are viable and fertile. In addition we could not discern any derangements in any of the major organ systems, including the nervous system, which we have studied in detail. Overall our results point to a functional redundancy of LANP's function, most likely provided by its closely related family members.Leucine-rich acidic nuclear protein (LANP or pp32 [for phosphoprotein with a molecular mass of 32 kDa]) is a member of the leucine-rich family of proteins (16-18). These proteins are involved in a variety of pathways including signaling, protein degradation, cytoskeletal dynamics, and morphogenesis, presumably based on the ability of the leucine-rich repeat (LRR) domains to serve as adapter sites for protein-protein interactions.For LANP, the hydrophobic LRRs reside in its N-terminal domain, giving LANP a globular head domain. The C-terminal domain, on the other hand, is extended and hydrophilic, engaging interactors by virtue of its ionic interactions (23,27,30,31).Several proteins have extensive homology to LANP, both in displaying LRRs in their N terminal domains and in demonstrating extended acidic tail domains. These proteins represent true LANP family members that have probably arisen by gene duplication. The nomenclature of LANP family members is confusing because the same protein has been given more than one name based on the context of isolation. Thus APRIL, an acronym derived from A protein rich in leucines, is also known as PAL-31, for proliferation-associated leucine-rich protein, MW 31kDa, and SSP-29, for silver-stainable protein with a molecular mass of 29 kDa (24,25,41). CPD1 (cerebellar postnatal development protein 1), another LANP family member, has been called LANP-like protein (LANP-L) (21, 28). Two human homologues of LANP/pp32 have been called pp32r1 and pp32r2 to signify that they are related (14,15). Besides having homology with these proteins, LANP family members also have limited homology to template-activating factor (TAF) proteins, TAF-1 alpha and beta (the latter being the product of the SET oncogene). The TAF-1 proteins, like the LANP family members, demonstrate long acidic C-terminal domains but, unlike LANP, do not display LRRs in their Nterminal doma...

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Differential expression of CPD1 during postnatal development in the mouse cerebellum

Cited by 26 publications

References 31 publications

Anp32e, a higher eukaryotic histone chaperone directs preferential recognition for H2A.Z

Anp32e, a higher eukaryotic histone chaperone directs preferential recognition for H2A.Z

Cpd-1 Null Mice Display a Subtle Neurological Phenotype

Generation and Characterization of LANP/pp32 Null Mice

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