Introduction of SHP-1

SHP-1 is a protein-tyrosine phosphatase with two Src homology 2 (SH2) domains. These SH2 domains determine which proteins SHP-1 associates with, but they also autoregulate the activity of the catalytic domain. In this report, we find that the murineSHP-1 transcript is processed to yield a series of alternatively spliced ​​in-frame transcripts, the majority of which exclude exons encoding one or the other SH2 domain. We have examined the corresponding protein isoforms in several ways. First, our measurements of V max and K munder different conditions indicate that the SH2 variants have elevated activity because of lessened autoregulation. Second, to ascertain whether regulation by the SH2 domains reflects intra- or intermolecular effects, we analyzed the state of SHP-1 by high performance liquid chromatography and sucrose density gradient centrifugation. Our results showed that SHP-1 is a monomer and, thus, is regulated in an intramolecular manner. Third, our analyses detected shape differences between SHP-1 and the active splice variant protein deleted of the amino-terminal SH2 domain ; ie SHP-1 was globular and resistant to proteolytic digestion, while the splice variant protein was "rod-shaped" and more susceptible to proteolytic digestion.
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