Related Experiment Video
Updated: Sep 25, 2026

Quantitative PCR-based Assay to Measure Sonic Hedgehog Signaling in Cellular Model of Ciliogenesis
Published on: January 31, 2025
The heterogeneous growth cone glycoprotein gp93 is identical to the signal regulatory protein SIRPalpha/SHPS-1/BIT
Xiaoxin X Wang1, Lawrence J Dangott, Karl H Pfenninger
1Department of Cellular and Structural Biology, University of Colorado School of Medicine, Denver 80262, USA.
Abstract:
Growth cone gp93 is a highly heterogeneous membrane glycoprotein with an Mr of about 93 kDa. It was purified from adult rat brain and microsequenced. The sequences of four different peptide fragments of gp93 matched those of the 'signal regulatory protein' SIRPalpha (also known as SHPS-1, BIT or P84), an Ig superfamily member. SIRPalpha contains a cytoplasmic tail that is a tyrosine kinase substrate and binds the protein tyrosine phosphatase SHP-2. SIRPalpha and gp93 also were immunochemically cross-reactive. A PCR strategy was used to determine whether gp93/SIRPalpha heterogeneity in the brain depended upon the presence of different transcripts and, thus, sequence heterogeneity. However, we observed only a single full-length transcript. A short splice variant also was detected. These data identify gp93 as the Ig superfamily member SIRPalpha. Together with our previous results, the data also demonstrate that, in rat brain, gp93/SIRPalpha heterogeneity is the result of differential glycosylation (plus phosphorylation), rather than sequence heterogeneity.
Related Concept Videos
Assembly of Signaling Complexes
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
Coat Assembly and GTPases
Coat assembly depends on the local availability of phosphatidylinositol phosphates or PIPs and GTP-binding proteins. Adaptor proteins, which link the coat proteins to the membrane, bind to these PIPs and play a crucial role in controlling...
Activation and Inactivation of G Proteins
Small GTPases - Ras and Rho
Three regulatory proteins control their activity:
GPI Anchoring of Proteins in the ER Membrane
GPI-anchor structure
A sequence of 11 enzymatic reactions results in the synthesis of the complete GPI anchor consisting of a hydrophobic and a hydrophilic portion. The hydrophobic portion comprises phosphatidylinositol, while the hydrophilic part comprises polar groups like phosphoethanolamine,...
Directing Proteins to the Rough Endoplasmic Reticulum

