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. Author manuscript; available in PMC: 2020 Feb 15.
Published in final edited form as: Trends Biochem Sci. 2019 Jun 27;44(10):885–896. doi: 10.1016/j.tibs.2019.05.004

Figure 2. Structural Characteristics of Transgelin-2.

Figure 2.

Human transgelin-2 contains an N terminal calponin-homolog (CH)-domain, an actin-binding motif (ABM), and a C terminal calponin-like repeated (CLR)-region. Transcript 202 encodes a polypeptide with 220 amino acids due to an extra (EX) N terminal sequence (SAFSLALALVSSPQPPPPIGM) after the initial methionine. The CH domain binds to metallothionein-2 (MT-2), ERK2, and TSG12. The ABM domain binds to actin. The C terminal CLR domain binds to ezrin. Transgelin-2 is regulated by phosphorylation at Ser-11, Ser-83, Thr-84, Ser-145, Ser-163, Thr-180, Ser-185, Thr-190, and Tyr-192. This phosphorylation is regulated by multiple extracellular factors (EGF and TGFβ) and intracellular kinases (ERK2, PKA, and PKC).