F
IPR008914

Phosphatidylethanolamine-binding protein

InterPro entry
Short namePEBP
Overlapping
homologous
superfamilies
 
family relationships

Description

The PEBP (PhosphatidylEthanolamine-Binding Protein) family is a highly conserved group of proteins that have been identified in numerous tissues in a wide variety of organisms, including bacteria, yeast, nematodes, plants, drosophila and mammals. The various functions described for members of this family include lipid binding, neuronal development
[1]
, serine protease inhibition
[2]
, the control of the morphological switch between shoot growth and flower structures
[3]
, and the regulation of several signalling pathways such as the MAP kinase pathway
[4]
, and the NF-kappaB pathway
[5]
. The control of the latter two pathways involves the PEBP protein RKIP, which interacts with MEK and Raf-1 to inhibit the MAP kinase pathway , and with TAK1, NIK, IKKalpha and IKKbeta to inhibit the NF-kappaB pathway. Other PEBP-like proteins that show strong structural homology to PEBP include Escherichia coli YBHB and YBCL
[6]
, the Rattus norvegicus (Rat) neuropeptide HCNP, and Antirrhinum majus (Garden snapdragon) protein centroradialis (CEN). Although their overall structures are similar, the members of the PEBP family bind very different substrates including phospholipids, opioids, and hydrophobic odorant molecules as well as having different oligomerization states (monomer/dimer/tetramer).

References

1.Peptides corresponding to the N- and C-terminal parts of PEBP are well-structured in solution: new insights into their possible interaction with partners in vivo. Vallee BS, Coadou G, Labbe H, Sy D, Vovelle F, Schoentgen F. J. Pept. Res. 61, 47-57, (2003). View articlePMID: 12492898

2.The phosphatidylethanolamine-binding protein is the prototype of a novel family of serine protease inhibitors. Hengst U, Albrecht H, Hess D, Monard D. J. Biol. Chem. 276, 535-40, (2001). View articlePMID: 11034991

3.The structure of Antirrhinum centroradialis protein (CEN) suggests a role as a kinase regulator. Banfield MJ, Brady RL. J. Mol. Biol. 297, 1159-70, (2000). View articlePMID: 10764580

4.Activation of Raf-1 signaling by protein kinase C through a mechanism involving Raf kinase inhibitory protein. Corbit KC, Trakul N, Eves EM, Diaz B, Marshall M, Rosner MR. J. Biol. Chem. 278, 13061-8, (2003). View articlePMID: 12551925

5.Raf kinase inhibitor protein interacts with NF-kappaB-inducing kinase and TAK1 and inhibits NF-kappaB activation. Yeung KC, Rose DW, Dhillon AS, Yaros D, Gustafsson M, Chatterjee D, McFerran B, Wyche J, Kolch W, Sedivy JM. Mol. Cell. Biol. 21, 7207-17, (2001). View articlePMID: 11585904

6.Crystal structures of YBHB and YBCL from Escherichia coli, two bacterial homologues to a Raf kinase inhibitor protein. Serre L, Pereira de Jesus K, Zelwer C, Bureaud N, Schoentgen F, Benedetti H. J. Mol. Biol. 310, 617-34, (2001). View articlePMID: 11439028

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