The BASP1 family of myristoylated proteins abundant in axonal termini. Primary structure analysis and physico-chemical properties

Mosevitsky, Mark I.; Capony, Jean‐Paul; Skladchikova, Galina; Novitskaya, Vera; Plekhanov, A. Yu.; Zakharov, V. V.

doi:10.1016/s0300-9084(97)80032-6

Biochimie

1997

DOI: 10.1016/s0300-9084(97)80032-6

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The BASP1 family of myristoylated proteins abundant in axonal termini. Primary structure analysis and physico-chemical properties

Mark I. Mosevitsky

Jean‐Paul Capony

Galina Skladchikova

et al.

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Cited by 67 publications

(78 citation statements)

References 49 publications

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“…It contains an N-terminal myristoylation signal and also several potential protein kinase C and casein kinase II recognition sites. The phosphorylation sites are nested within PEST sequences, which are characteristic of high-turnover proteins (27). We also note that BASP1 contains a nuclear localization sequence close to the N terminus.…”

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confidence: 77%

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BASP1 Is a Transcriptional Cosuppressor for the Wilms' Tumor Suppressor Protein WT1

Carpenter

Hill

Charalambous

et al. 2004

Molecular and Cellular Biology

124

156

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The Wilms' tumor suppressor protein WT1 is a transcriptional regulator that plays a key role in the development of the kidneys. The transcriptional activation domain of WT1 is subject to regulation by a suppression region within the N terminus of WT1. Using a functional assay, we provide direct evidence that this requires a transcriptional cosuppressor, which we identify as brain acid soluble protein 1 (BASP1). WT1 and BASP1 associate within the nuclei of cells that naturally express both proteins. BASP1 can confer WT1 cosuppressor activity in transfection assays, and elimination of endogenous BASP1 expression augments transcriptional activation by WT1. BASP1 is present in the developing nephron structures of the embryonic kidney and, coincident with that of WT1, its expression is restricted to the highly specialized podocyte cells of the adult kidney. Taken together, our results show that BASP1 is a WT1-associated factor that can regulate WT1 transcriptional activity.Wilms' tumor, a pediatric malignancy of the kidneys, is the most common solid childhood tumor (reviewed in references 4, 7, 20, 30, and 33). The isolation of genes associated with Wilms' tumor led to the identification of a zinc finger protein, WT1. Subsequently, WT1 was shown to be a transcriptional regulator with putative target genes including those for growth factors and regulators of cell division (5,6,18,21). Approximately 15% of sporadic Wilms' tumors have been found to contain mutations in WT1, while others show aberrant WT1 expression (33).WT1 knockout mice (homozygous null) do not survive gestation, displaying absence or incorrect development of the kidney, gonads, spleen, heart, diaphragm, and retinal ganglia (12,14,35). These findings confirm a major role for WT1 in the formation of the genitourinary system and also a wider role in the development of other tissues.Alternative splicing, RNA editing, and an alternative translation start codon combine to produce a plethora of WT1 isoforms (reviewed in reference 33). One alternative splice inserts three amino acids (KTS) between zinc fingers three and four, resulting in a form of WT1 that associates with RNA processing factors and localizes to regions of RNA processing in the nucleus (17). Thus, the ϩKTS and ϪKTS isoforms of WT1 have been proposed to function in RNA processing and transcription, respectively. These isoforms have both overlapping and distinct roles during development (9, 10). Interestingly, the ϩKTS isoform of WT1 plays the dominant role in the development of the gonad, while the ϪKTS isoform has a more extensive function in kidney formation.The other alternative splice inserts 17 amino acids N terminal to the WT1 zinc fingers and has been shown to have effects on both cell division and cell survival (15,31,32). Specific elimination of this isoform of WT1 in mice does not result in any obvious defects in genitourinary development, suggesting that it may be required specifically for a tumor suppressor role or that it performs a subtle function (28).Several studies have shown ...

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confidence: 77%

“…BASP1 was previously purified as an N-terminally myristoylated protein from the cytoplasm of brain cells (27). It belongs to a group of factors that includes neuronal tissue-enriched acidic protein (NAP22) (29) and neuronal growth-associated protein (GAP-43) (38).…”

mentioning

confidence: 99%

BASP1 Is a Transcriptional Cosuppressor for the Wilms' Tumor Suppressor Protein WT1

Carpenter

Hill

Charalambous

et al. 2004

Molecular and Cellular Biology

124

156

View full text Add to dashboard Cite

show abstract

“…12 It was initially described as a brain-specific protein, 10,11 but later studies revealed that BASP1 is also expressed by human endothelium, 13 developing mammary gland, kidney, testis, and lymphoid tissues. [12][13][14][15][16] BASP1 is involved in cytoskeletal and lipid raft dynamics, as well as in the nuclear regulation of transcription. However, a role in apoptosis has not been previously reported.…”

mentioning

confidence: 99%

“…Reversible phosphorylation of ED by protein kinase C modulates these interactions. 12 In the plasma membrane BASP1 localizes to lipid rafts and may influence the behavior and composition of the membrane. 17 In addition, BASP1 promotes actin dynamics, including loss of stress fibers and bleb formation.…”

mentioning

confidence: 99%

BASP1 Promotes Apoptosis in Diabetic Nephropathy

Sanchez-Niño¹,

Sanz

Lorz³

et al. 2010

Journal of the American Society of Nephrology

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Apoptosis contributes to the development of diabetic nephropathy (DN), but the mechanisms that lead to diabetes-induced cell death are not fully understood. Here, we combined a functional genomics screen for cDNAs that induce apoptosis in vitro with transcriptional profiling of renal biopsies from patients with DN. Twelve of the 138 full-length cDNAs that induced cell death in human embryonic kidney cells matched upregulated mRNA transcripts in tissue from human DN. Confirmatory screens identified induction of BASP1 in tubular cross sections of human DN tissue. In vitro, apoptosis-inducing conditions such as serum deprivation, high concentrations of glucose, and proinflammatory cytokines increased BASP1 mRNA and protein in human tubular epithelial cells. In normal cells, BASP1 localized to the cytoplasm, but in apoptotic cells, it colocalized with actin in the periphery. Overexpression of BASP1 induced cell death with features of apoptosis; conversely, small interfering RNA (siRNA)-mediated knockdown of BASP1 protected tubular cells from apoptosis. Supporting possible involvement of BASP1 in renal disease other than DN, we also observed significant upregulation of renal BASP1 in spontaneously hypertensive rats and a trend toward increased tubulointerstitial BASP1 mRNA in human hypertensive nephropathy. In summary, a combined functional genomics approach identified BASP1 as a proapoptotic factor in DN and possibly also in hypertensive nephropathy.

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“…The myristoylation of NAP-22 was independently confirmed by using a vaculovirus expression system and by the analysis using electrospray mass spectrometry. Also, the membrane localization of NAP-22 was partly ascribed to the myristoylation in its N terminus (30,32,33). Further * This study was supported by Grants-in-Aid for Scientific Research on Priority Areas 07279222 and for Scientific Research (B) 11490022 from the Ministry of Education, Science, Sports, and Culture of Japan.…”

mentioning

confidence: 99%

Cholesterol-dependent Localization of NAP-22 on a Neuronal Membrane Microdomain (Raft)

Maékawa¹,

Sato²,

Kitajima³

et al. 1999

Journal of Biological Chemistry

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A membrane microdomain called raft has been under extensive study since the assembly of various signaltransducing molecules into this region has been envisaged. This domain is isolated as a low buoyant membrane fraction after the extraction with a nonionic detergent such as Triton X-100. The characteristic low density of this fraction is ascribed to the enrichment of several lipids including cholesterol. To clear the molecular mechanism of raft formation, several extraction methods were applied to solubilize raft components. Cholesterol extraction using methyl-␤-cyclodextrin was found to be effective to solubilize NAP-22, a neuronenriched Ca 2؉ -dependent calmodulin-binding protein as well as one of the main protein components of brain raft. Purified NAP-22 bound to the liposomes that were made from phosphatidylcholine and cholesterol. This binding was dependent on the amount of cholesterol in liposomes. Calmodulin inhibited this binding in a dosedependent manner. These results suggest that the presence of a calcium-dependent regulatory mechanism works on the assembly of raft within the neuron.

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The BASP1 family of myristoylated proteins abundant in axonal termini. Primary structure analysis and physico-chemical properties

Cited by 67 publications

References 49 publications

BASP1 Is a Transcriptional Cosuppressor for the Wilms' Tumor Suppressor Protein WT1

BASP1 Is a Transcriptional Cosuppressor for the Wilms' Tumor Suppressor Protein WT1

BASP1 Promotes Apoptosis in Diabetic Nephropathy

Cholesterol-dependent Localization of NAP-22 on a Neuronal Membrane Microdomain (Raft)

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