Nuclear localization of Myomesin-1: possible functions.

Myomesin-I (also known as Skelemin) is a approximately 185 kDa protein, which is highly expressed in striated muscle. It contains the prototypic class-I (type-III fibronectin) and class-II (C2-immunoglobulin) motifs. Previous studies have shown the presence of Myomesin-I at the M-line of the sarcomere, where it is thought to interact with thick filament constituents.

Analysis of Fyn function in hemostasis and alphaIIbbeta3-integrin signaling.

Recent studies have shown that Src-family kinases (SFKs) play an important role in mediating integrin signalling, and the beta3 subunit of alphaIIbbeta3 integrin has been shown to interact with multiple SFK members. Here, we analyzed the interactions and functional consequences of Fyn and Src binding to alphaIIbbeta3. Fyn associated with the beta3 subunit in resting and thrombin-aggregated platelets, whereas interaction between Src and alphaIIbbeta3 was seen predominantly in resting but not in thrombin-aggregated platelets.