http://orcid.org/0000-0002-0630-4027
Figures & data
Figure 1. Protein Structure, gene organization and mRNA expression of Lamp2A in fish (A) Schematic drawing of the structure of vertebrate LAMP2A. The human LAMP2A is used as reference. It shows a lumenal region comprising 2 N-glycosylated LAMP domains of approximately 160 residues (each with 2 disulfide bonds, S-S) separated by a proline-rich, O-glycosylated ‘hinge’ region of approximately 30 amino acid residues [Citation21]. O- and N-linked glycosylation are indicated in green and red, respectively. The transmembrane (TM) domain, harboring 2 glycine residues (red G) involved in the multimeric pattern of LAMP2A, is followed by a short, C-terminal cytosolic tail that is comprised of 4 positively-charged amino acids (KHHH in blue) required for the binding of substrate proteins as well as motifs for lysosomal targeting (in green). The schematic drawing of fish Lamp2A has been done on the basis of sequence complementarity with the human LAMP2A. Potential O- and N-linked glycosylation are indicated in light green and pink, respectively. Sequence alignment of the boxed region of the 3 LAMP2/Lamp2 variants is shown below. The positively-charged amino acids required for the binding of substrate proteins are colored in blue. The GY dipeptide as well as the hydrophobic F required for targeting of LAMP2A to lysosomes are in green. The glycine residues (G) involved in the multimeric pattern of LAMP2A are in red. (B) The genomic structure of LAMP2/lamp2 is conserved in vertebrates and contains the 3 alternative exons (B, A and C) encoding the transmembrane domain and cytoplasmic tail specific for each isoform. The size of exons (in base pairs) is shown in italics below or above each exon. (C) Data from RNAseq show that lamp2a is expressed in different tissues of a large number of ray-finned fish. Relative expression of lamp2a was expressed in number of reads per kilobase per million reads per species, after normalization of data by the total number of sequences obtained for each tissue and species. The obtained values were then log transformed and centered to the median (set at 0.00). Ac, Amia calva (bowfin); Lo, Lepisosteus oculatus (spotted gar); Aa, Anguilla anguilla (European eel); Gp, Gnathonemus petersi (elephantnose fish); Aal, Alosa alosa (allis shad); Ph, Pangasianodon hypophthalmus (striped Catfish); Am, Astyanax mexicanus (cave Mexican tetra); El, Esox lucius (northern pike); Up, Umbra pygmae (eastern mudminnow); Tt, Thymallus thymallus (grayling); Cl, Coregonus lavaretus (European whitefish); Cc, Coregonus clupeaformis (American whitefish); St, Salmo trutta (brown trout); Om, Oncorhynchus mykiss (rainbow trout); Sf, Salvelinus fontinalis (brook trout); Gm, Gadus morhua (Atlantic cod); Ol, Oryzias latipes (medaka).
![Figure 1. Protein Structure, gene organization and mRNA expression of Lamp2A in fish (A) Schematic drawing of the structure of vertebrate LAMP2A. The human LAMP2A is used as reference. It shows a lumenal region comprising 2 N-glycosylated LAMP domains of approximately 160 residues (each with 2 disulfide bonds, S-S) separated by a proline-rich, O-glycosylated ‘hinge’ region of approximately 30 amino acid residues [Citation21]. O- and N-linked glycosylation are indicated in green and red, respectively. The transmembrane (TM) domain, harboring 2 glycine residues (red G) involved in the multimeric pattern of LAMP2A, is followed by a short, C-terminal cytosolic tail that is comprised of 4 positively-charged amino acids (KHHH in blue) required for the binding of substrate proteins as well as motifs for lysosomal targeting (in green). The schematic drawing of fish Lamp2A has been done on the basis of sequence complementarity with the human LAMP2A. Potential O- and N-linked glycosylation are indicated in light green and pink, respectively. Sequence alignment of the boxed region of the 3 LAMP2/Lamp2 variants is shown below. The positively-charged amino acids required for the binding of substrate proteins are colored in blue. The GY dipeptide as well as the hydrophobic F required for targeting of LAMP2A to lysosomes are in green. The glycine residues (G) involved in the multimeric pattern of LAMP2A are in red. (B) The genomic structure of LAMP2/lamp2 is conserved in vertebrates and contains the 3 alternative exons (B, A and C) encoding the transmembrane domain and cytoplasmic tail specific for each isoform. The size of exons (in base pairs) is shown in italics below or above each exon. (C) Data from RNAseq show that lamp2a is expressed in different tissues of a large number of ray-finned fish. Relative expression of lamp2a was expressed in number of reads per kilobase per million reads per species, after normalization of data by the total number of sequences obtained for each tissue and species. The obtained values were then log transformed and centered to the median (set at 0.00). Ac, Amia calva (bowfin); Lo, Lepisosteus oculatus (spotted gar); Aa, Anguilla anguilla (European eel); Gp, Gnathonemus petersi (elephantnose fish); Aal, Alosa alosa (allis shad); Ph, Pangasianodon hypophthalmus (striped Catfish); Am, Astyanax mexicanus (cave Mexican tetra); El, Esox lucius (northern pike); Up, Umbra pygmae (eastern mudminnow); Tt, Thymallus thymallus (grayling); Cl, Coregonus lavaretus (European whitefish); Cc, Coregonus clupeaformis (American whitefish); St, Salmo trutta (brown trout); Om, Oncorhynchus mykiss (rainbow trout); Sf, Salvelinus fontinalis (brook trout); Gm, Gadus morhua (Atlantic cod); Ol, Oryzias latipes (medaka).](/cms/asset/e8c208ab-64b6-4ddb-a2d6-48396b66596e/kaup_a_1460021_f0001_c.jpg)
