ArticleEndocrinology2025
Identification of βIIΣ1-Spectrin as a Binding Partner of the GH-regulated Human Obesity Scaffold Protein SH2B1.
Article in Endocrinology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
SH2B1β is a multifunctional scaffold protein that modulates cytoskeletal processes such as cellular motility and neurite outgrowth. To identify novel SH2B1β-interacting proteins involved in these processes, a yeast 2-hybrid assay was performed. The C-terminal 159 residues of the cytoskeleton structural protein, βIIΣ1-spectrin, interacted with the N-terminal 260 residues of SH2B1β, a region implicated in SH2B1β enhancement of cell motility and localization at the plasma membrane. The interaction between SH2B1β and βIIΣ1-spectrin (2205-2363) requires residues 1 through 150 in SH2B1β, with residues 105 through 120 playing a key role. While βIIΣ1-spectrin (2205-2363) was expressed throughout the cell, it colocalized with SH2B1β when coexpressed with SH2B1β mutants with varied intracellular localizations. The SH2B1β-βIIΣ1-spectrin (2205-2363) interaction impaired the ability of SH2B1β to enter the nucleus. A slightly larger βIIΣ1-spectrin fragment (2170-2363) with an intact pleckstrin homology domain localized primarily to the plasma membrane and cytoplasm, similar to SH2B1β. Similarly, full-length βIIΣ1-spectrin colocalized at the plasma membrane and cytoplasm with SH2B1β as well as the SH2B1β-regulated tyrosine kinase, JAK2. Phosphorylation of spectrins has been shown to regulate their localization and function. Coexpression of βIIΣ1-spectrin, JAK2, and SH2B1β resulted in SH2B1β-dependent tyrosyl phosphorylation of βIIΣ1-spectrin. Finally, stimulation with GH induced formation of an endogenous complex containing βII-spectrin, SH2B1, and JAK2 in 3T3-F442A cells and increased tyrosyl phosphorylation of βII-spectrin. Our results identify a novel interaction between SH2B1β, βIIΣ1-spectrin, and JAK2 resulting in JAK2- and SHB1-dependent tyrosyl phosphorylation of βII-spectrin. This raises the possibility that the many other ligand-activated tyrosine kinases that signal through SH2B1 form similar complexes with βIIΣ1-spectrin.
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