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. 2021 Sep 10;9:690397. doi: 10.3389/fcell.2021.690397

FIGURE 1.

FIGURE 1

TβRII-SE splice variant is produced by human cells and is able to generate a truncated soluble protein. (A) TβRII-SE was originally detected in human lymphocytes as a 433-bp band after end point RT-PCR. (B) Primers design to amplify the coding sequence of the endoplasmic reticulum signal peptide (SP), extracellular domain (ECD), and transmembrane domain (TMD) of membrane-bound TβRII splice variants. (C) End point RT-PCR of PBMC isolated CD3+, CD19+, CD14+ cells, and granulocytes; and human adipose stromal cells (hASC), immortalized T lymphocyte cell line (Jurkat), and human embryonic kidney cell line containing the SV40 T-antigen (293T). (D) Partial nucleotide sequence alignment of TβRII and TβRII-SE depicting the stretch absent in the new splice variant. (E) Predicted amino acid sequence alignment of TβRII and TβRII-SE showing the presence of the SP and predicted PTM in both isoforms, and the absence of the transmembrane domain (TMD) in TβRII-SE. C-terminal 13-amino-acid stretch distinctive of TβRII-SE is shown in bold. P, kinase-specific phosphorylation; Glycat, glycation; SUMO, non-consensus sumoylation.