D
IPR053793

PB1-like domain

InterPro entry
Short namePB1-like
domain relationships

Description

The PB1 (Phox and Bem1) domain, comprising about 80 amino acid residues, is conserved among animals, fungi, amoebas, and plants. It functions as a protein binding module through PB1-mediated heterodimerization or homo-oligomerization
[3, 2, 1, 4]
. The PB1 domain is found in several signaling proteins including:


- Mammalian MEK5, a MAP kinase kinase implicated in epidermal growth factor-induced cell proliferation.

- Mammalian Sequestosome-1 (Sqstm1) or p62/ZIP, a protein linking the zeta isoform of protein kinase C to RIP and/or potassium channels.

- Mammalian neutrophil cytosol factor 4 (NCF-4) or p40(phox), a cytosolic factor of the superoxide-generating NADPH oxidase in phagocytes.

- Mammalian neutrophil cytosol factor 2 (NCF-2) or p67(phox), an oxidase activator.

- Yeast bud emergence protein 1 (Bem1), necessary for cell polarization during vegetative growth.

- Yeast cell division control protein 24 (CDC24), a guanine nucleotide exchange factor (GEF) for the small GTPase CDC42.

- Plant AUXIN RESPONSE FACTOR (ARF) transcription factor family, regulates gene expression in response to auxin.

The PB1 domains adopt an ubiquitin-like β-grasp fold, containing two α-helices and a mixed five-stranded β-sheet. PB1 domains may display an acidic surface (type I), a basic surface (tape II), or both surfaces (type I/II) on opposite faces of the domain structure to allow for front-to-back orientation of multiple PB1 domains
[3, 2, 1, 4]
.

References

1.Structure and ligand recognition of the PB1 domain: a novel protein module binding to the PC motif. Terasawa H, Noda Y, Ito T, Hatanaka H, Ichikawa S, Ogura K, Sumimoto H, Inagaki F. EMBO J. 20, 3947-56, (2001). View articlePMID: 11483498

2.Structure of a cell polarity regulator, a complex between atypical PKC and Par6 PB1 domains. Hirano Y, Yoshinaga S, Takeya R, Suzuki NN, Horiuchi M, Kohjima M, Sumimoto H, Inagaki F. J. Biol. Chem. 280, 9653-61, (2005). View articlePMID: 15590654

3.Structure and function of the PB1 domain, a protein interaction module conserved in animals, fungi, amoebas, and plants. Sumimoto H, Kamakura S, Ito T. Sci. STKE 2007, re6, (2007). View articlePMID: 17726178

4.Molecular basis for AUXIN RESPONSE FACTOR protein interaction and the control of auxin response repression. Korasick DA, Westfall CS, Lee SG, Nanao MH, Dumas R, Hagen G, Guilfoyle TJ, Jez JM, Strader LC. Proc. Natl. Acad. Sci. U.S.A. 111, 5427-32, (2014). View articlePMID: 24706860

Cross References

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