The Anp32 family of proteins containing leucine-rich repeats
Herein we describe the characteristic features of the Anp32 family represented by the cerebellar leucine-rich repeat protein (Lanp) and the cerebellar developmental-regulated protein 1 (Cpd1). The Anp32 family consists of 32 evolutionarily-conserved proteins and is included within the superfamily of...
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2005
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| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_14734222_v4_n1_p7_Matilla http://hdl.handle.net/20.500.12110/paper_14734222_v4_n1_p7_Matilla |
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paper:paper_14734222_v4_n1_p7_Matilla2023-06-08T16:17:35Z The Anp32 family of proteins containing leucine-rich repeats Radrizzani Helguera, Martín Anp32 Cpd1 Lanp Leucine-rich repeats Signal transduction adenine cytosine leucine nuclear protein protein anp32 protein cpd1 protein lanp regulator protein unclassified drug amino acid sequence cell adhesion cell structure cerebellum cytoskeleton evolution gene expression human morphogenesis nervous system development nucleotide sequence priority journal protein expression protein function protein localization protein motif protein protein interaction review sequence analysis signal transduction structure analysis tandem repeat tissue distribution Amino Acid Sequence Animals Cerebellum Humans Molecular Sequence Data Nerve Tissue Proteins Neurodegenerative Diseases Nuclear Proteins Phylogeny Protein Structure, Tertiary Proteins Sequence Alignment Sequence Homology, Amino Acid Herein we describe the characteristic features of the Anp32 family represented by the cerebellar leucine-rich repeat protein (Lanp) and the cerebellar developmental-regulated protein 1 (Cpd1). The Anp32 family consists of 32 evolutionarily-conserved proteins and is included within the superfamily of leucine-rich repeat (LRR) proteins characterized by the presence of tandem arrays of a LRR, a structural motif implicated in the mediation of protein-protein interactions. We describe three novel human Anp32 proteins, reveal the evolutionary relationships of the members of the Anp32 family, provide insights into their biochemical and structural properties, and review their macromolecular interactions, substrate specificities, tissue distribution/expression patterns, and physiological and pathological roles. Recent findings indicate a conserved role of members of the Anp32 family during evolution in the modulation of cell signalling and transduction of gene expression to regulate the morphology and dynamics of the cytoskeleton, cell adhesion, neural development or cerebellar morphogenesis. © 2005 Taylor & Francis Group Ltd. Fil:Radrizzani, M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 2005 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_14734222_v4_n1_p7_Matilla http://hdl.handle.net/20.500.12110/paper_14734222_v4_n1_p7_Matilla |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
Anp32 Cpd1 Lanp Leucine-rich repeats Signal transduction adenine cytosine leucine nuclear protein protein anp32 protein cpd1 protein lanp regulator protein unclassified drug amino acid sequence cell adhesion cell structure cerebellum cytoskeleton evolution gene expression human morphogenesis nervous system development nucleotide sequence priority journal protein expression protein function protein localization protein motif protein protein interaction review sequence analysis signal transduction structure analysis tandem repeat tissue distribution Amino Acid Sequence Animals Cerebellum Humans Molecular Sequence Data Nerve Tissue Proteins Neurodegenerative Diseases Nuclear Proteins Phylogeny Protein Structure, Tertiary Proteins Sequence Alignment Sequence Homology, Amino Acid |
| spellingShingle |
Anp32 Cpd1 Lanp Leucine-rich repeats Signal transduction adenine cytosine leucine nuclear protein protein anp32 protein cpd1 protein lanp regulator protein unclassified drug amino acid sequence cell adhesion cell structure cerebellum cytoskeleton evolution gene expression human morphogenesis nervous system development nucleotide sequence priority journal protein expression protein function protein localization protein motif protein protein interaction review sequence analysis signal transduction structure analysis tandem repeat tissue distribution Amino Acid Sequence Animals Cerebellum Humans Molecular Sequence Data Nerve Tissue Proteins Neurodegenerative Diseases Nuclear Proteins Phylogeny Protein Structure, Tertiary Proteins Sequence Alignment Sequence Homology, Amino Acid Radrizzani Helguera, Martín The Anp32 family of proteins containing leucine-rich repeats |
| topic_facet |
Anp32 Cpd1 Lanp Leucine-rich repeats Signal transduction adenine cytosine leucine nuclear protein protein anp32 protein cpd1 protein lanp regulator protein unclassified drug amino acid sequence cell adhesion cell structure cerebellum cytoskeleton evolution gene expression human morphogenesis nervous system development nucleotide sequence priority journal protein expression protein function protein localization protein motif protein protein interaction review sequence analysis signal transduction structure analysis tandem repeat tissue distribution Amino Acid Sequence Animals Cerebellum Humans Molecular Sequence Data Nerve Tissue Proteins Neurodegenerative Diseases Nuclear Proteins Phylogeny Protein Structure, Tertiary Proteins Sequence Alignment Sequence Homology, Amino Acid |
| description |
Herein we describe the characteristic features of the Anp32 family represented by the cerebellar leucine-rich repeat protein (Lanp) and the cerebellar developmental-regulated protein 1 (Cpd1). The Anp32 family consists of 32 evolutionarily-conserved proteins and is included within the superfamily of leucine-rich repeat (LRR) proteins characterized by the presence of tandem arrays of a LRR, a structural motif implicated in the mediation of protein-protein interactions. We describe three novel human Anp32 proteins, reveal the evolutionary relationships of the members of the Anp32 family, provide insights into their biochemical and structural properties, and review their macromolecular interactions, substrate specificities, tissue distribution/expression patterns, and physiological and pathological roles. Recent findings indicate a conserved role of members of the Anp32 family during evolution in the modulation of cell signalling and transduction of gene expression to regulate the morphology and dynamics of the cytoskeleton, cell adhesion, neural development or cerebellar morphogenesis. © 2005 Taylor & Francis Group Ltd. |
| author |
Radrizzani Helguera, Martín |
| author_facet |
Radrizzani Helguera, Martín |
| author_sort |
Radrizzani Helguera, Martín |
| title |
The Anp32 family of proteins containing leucine-rich repeats |
| title_short |
The Anp32 family of proteins containing leucine-rich repeats |
| title_full |
The Anp32 family of proteins containing leucine-rich repeats |
| title_fullStr |
The Anp32 family of proteins containing leucine-rich repeats |
| title_full_unstemmed |
The Anp32 family of proteins containing leucine-rich repeats |
| title_sort |
anp32 family of proteins containing leucine-rich repeats |
| publishDate |
2005 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_14734222_v4_n1_p7_Matilla http://hdl.handle.net/20.500.12110/paper_14734222_v4_n1_p7_Matilla |
| work_keys_str_mv |
AT radrizzanihelgueramartin theanp32familyofproteinscontainingleucinerichrepeats AT radrizzanihelgueramartin anp32familyofproteinscontainingleucinerichrepeats |
| _version_ |
1768544611716825088 |