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The proline‐rich region of glyceraldehyde‐3‐phosphate dehydrogenase from human sperm may bind SH3 domains, as revealed by a bioinformatic study of low‐complexity protein segments
Author(s) -
Tatjewski Marcin,
Gruca Aleksandra,
Plewczynski Dariusz,
Grynberg Marcin
Publication year - 2016
Publication title -
molecular reproduction and development
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.745
H-Index - 105
eISSN - 1098-2795
pISSN - 1040-452X
DOI - 10.1002/mrd.22606
Subject(s) - biology , sh3 domain , leucine rich repeat , signal transduction , proline dehydrogenase , peptide sequence , sh2 domain , biochemistry , kinase , proline , microbiology and biotechnology , amino acid , gene , receptor tyrosine kinase
SUMMARY Glyceraldehyde‐3‐phosphate dehydrogenase from human sperm (GAPDHS) provides energy to the sperm flagellum, and is therefore essential for sperm motility and male fertility. This isoform is distinct from somatic GAPDH, not only in being specific for the testis but also because it contains an additional amino‐terminal region that encodes a proline‐rich motif that is known to bind to the fibrous sheath of the sperm tail. By conducting a large‐scale sequence comparison on low‐complexity sequences available in databases, we identified a strong similarity between the proline‐rich motif from GAPDHS and the proline‐rich sequence from Ena/vasodilator‐stimulated phosphoprotein‐like (EVL), which is known to bind an SH3 domain of dynamin‐binding protein (DNMBP). The putative binding partners of the proline‐rich GAPDHS motif include SH3 domain‐binding protein 4 (SH3BP4) and the IL2‐inducible T‐cell kinase/tyrosine‐protein kinase ITK/TSK (ITK). This result implies that GAPDHS participates in specific signal‐transduction pathways. Gene Ontology category‐enrichment analysis showed several functional classes shared by both proteins, of which the most interesting ones are related to signal transduction and regulation of hydrolysis. Furthermore, a mutation of one EVL proline to leucine is known to cause colorectal cancer, suggesting that mutation of homologous amino acid residue in the GAPDHS motif may be functionally deleterious. Mol. Reprod. Dev. 83: 144–148, 2016. © 2015 Wiley Periodicals, Inc .