Disease relevance of BASP1

• BASP1 is a transcriptional cosuppressor for the Wilms' tumor suppressor protein WT1 [1].
• Based on the N-terminal amino acid sequence alignment of CAP-23/NAP-22 and other myristoylated proteins, including the Nef protein from human immunodeficiency virus (HIV), we proposed a new hypothesis that the protein myristoylation plays important roles in protein-calmodulin interactions [2].
• Expression and myristoylation of NAP-22 using a baculovirus transfer vector system [3].

High impact information on BASP1

• Taken together, our results show that BASP1 is a WT1-associated factor that can regulate WT1 transcriptional activity [1].
• In addition, the expression of growth-associated proteins such as GAP-43 and CAP-23 in neurons lowers the threshold for nerve sprouting and potentiates its vigour [4].
• Furthermore, phosphorylation of CAP-23/NAP-22 by protein kinase C was also found myristoylation-dependent, suggesting the importance of myristoylation in protein-protein interactions [5].
• In light of these facts, we consider GAP-43, MARCKS, and BASP1 both separately and in conjunction [6].
• Our results demonstrated that the NAP-22 peptide interacts with membranes in a concentration-dependent manner, preferentially inserting into DOPC (l(d)) domains [7].

Chemical compound and disease context of BASP1

• In this study, we showed the myristoylation of NAP-22 using a Baculovirus expression system and also showed a liposome binding ability of the expressed protein in Escherichia coli [3].

Biological context of BASP1

• In this work, complete amino acid sequences of bovine BASP1 and human BASP1 were established [8].
• Several proteins harbor putative post-translational modifications that favor its localization in the lipid-raft environment, such as GPI (alkaline phosphatase and 5'-nucleotidase) and myristoylation (BASP1 and MARCKS) [9].
• Assignment of brain acid-soluble protein 1 (BASP1) to human chromosome 5p15.1-->p14, differential expression in human cancer cell lines as a result of alterations in gene dosage [10].
• Several important protein motifs, including myristoylation and phosphorylation sites, are well conserved in sequences and positions in all three mammalian NAP-22 proteins and chicken CAP-23 proteins [11].
• The peptide sequence analysis also showed that NAP-22 has a consensus sequence of N-myristoylation and the presence of polybasic domain in its N-terminal region [3].

Anatomical context of BASP1

• 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 [1].
• Proteins BASP1 and GAP-43/B-50, which are abundant in nerve endings, show a number of similar physico-chemical properties [8].
• Unlike GAP-43/B-50, BASP1 is present in high amounts also in some non-nervous tissues: testis, kidney and lymphoid organs (spleen, thymus) [8].
• They also share 45% and 41% amino acid sequence identities with chicken CAP-23 (23 kDa cytoskeleton associated protein) [11].
• A protein, NAP-22, present in high abundance in the synaptic cell membrane and synaptic vesicle, promotes the formation of cholesterol crystallites in lipid mixtures in which cholesterol would be completely dissolved in the membrane in the absence of protein [12].

Associations of BASP1 with chemical compounds

• The arrangement of cholesterol in membranes and binding of NAP-22 [12].
• This finding, along with effects of the protein on the phase transitions of mixtures of phosphatidylcholine (PC) and cholesterol indicate that NAP-22 facilitates the formation of cholesterol-rich domains [12].
• In vivo mitochondrial protein synthesis in CAP-23 cells was inhibited little, if any, by chloramphenicol, and the variant showed and partial cross resistance to mikamycin and carbomycin [13].

Other interactions of BASP1

• Nerve ending "signal" proteins GAP-43, MARCKS, and BASP1 [6].
• Cholesterol-dependent partitioning of PtdIns(4,5)P2 into membrane domains by the N-terminal fragment of NAP-22 (neuronal axonal myristoylated membrane protein of 22 kDa) [14].

Analytical, diagnostic and therapeutic context of BASP1

• Tracking peptide-membrane interactions: Insights from in situ coupled confocal-atomic force microscopy imaging of NAP-22 peptide insertion and assembly [7].
• We have applied in situ correlated atomic force and confocal microscopies to characterize the interaction of the NAP-22 peptide with model membranes prepared as supported planar bilayers containing both liquid-ordered and liquid-disordered domains [7].
• No obvious morphological changes in mitochondria were observed by electron microscopy of thin sections of CAP-23 cells [13].

References