H
IPR011333

SKP1/BTB/POZ domain superfamily

InterPro entry
Short nameSKP1/BTB/POZ_sf
Overlapping entries
 
BTB/POZ domain (IPR000210)

Description

The BTB (for BR-C, ttk and bab)
[1]
or POZ (for Pox virus and Zinc finger)
[2, 3]
domain is a versatile protein-protein interaction motif involved in many cellular functions, including transcriptional regulation, cytoskeleton dynamics, ion channel assembly and gating, and targeting proteins for ubiquitination
[4]
. The BTB domain can occur alongside other domains: BTB-zinc finger (BTB-ZF), BTB-BACK-Kelch (BBK), voltage-gated potassium channel T1 (T1-Kv)
[5]
, MATH-BTB, BTB-NPH3 and BTB-BACK-PHR (BBP). Other proteins, such as Skp1 and ElonginC, consist almost exclusively of the core BTB fold. In all of these protein families, the BTB core fold is structurally conserved, consisting of a 2-layer α/β topology where a cluster of α-helices is flanked by short β-sheets
[6]
. POZ domains from several zinc finger proteins have been shown to mediate transcriptional repression and to interact with components of histone deacetylase co-repressor complexes including N-CoR and SMRT
[7, 8, 9]
. The POZ or BTB domain is also known as BR-C/Ttk or ZiN.

This entry includes the BTB/POZ domain, as well as Skp1 N-terminal region which has an α/β structure similar to that of the BTB/POZ domain fold
[5, 10]
.

References

1.The BTB domain, found primarily in zinc finger proteins, defines an evolutionarily conserved family that includes several developmentally regulated genes in Drosophila. Zollman S, Godt D, Prive GG, Couderc JL, Laski FA. Proc. Natl. Acad. Sci. U.S.A. 91, 10717-21, (1994). View articlePMID: 7938017

2.The POZ domain: a conserved protein-protein interaction motif. Bardwell VJ, Treisman R. Genes Dev. 8, 1664-77, (1994). View articlePMID: 7958847

3.Functional analysis of the role of POK transcriptional repressors. Costoya JA. 6, 8-18, (2007). View articlePMID: 17384421

4.Sequence and structural analysis of BTB domain proteins. Stogios PJ, Downs GS, Jauhal JJ, Nandra SK, Prive GG. Genome Biol. 6, R82, (2005). View articlePMID: 16207353

5.Fold prediction and evolutionary analysis of the POZ domain: structural and evolutionary relationship with the potassium channel tetramerization domain. Aravind L, Koonin EV. J. Mol. Biol. 285, 1353-61, (1999). View articlePMID: 9917379

6.Crystal structure of the BTB domain from PLZF. Ahmad KF, Engel CK, Prive GG. Proc. Natl. Acad. Sci. U.S.A. 95, 12123-8, (1998). View articlePMID: 9770450

7.The LAZ3/BCL6 oncogene encodes a sequence-specific transcriptional inhibitor: a novel function for the BTB/POZ domain as an autonomous repressing domain. Deweindt C, Albagli O, Bernardin F, Dhordain P, Quief S, Lantoine D, Kerckaert JP, Leprince D. Cell Growth Differ. 6, 1495-503, (1995). View articlePMID: 9019154

8.The BCL-6 POZ domain and other POZ domains interact with the co-repressors N-CoR and SMRT. Huynh KD, Bardwell VJ. Oncogene 17, 2473-84, (1998). View articlePMID: 9824158

9.Components of the SMRT corepressor complex exhibit distinctive interactions with the POZ domain oncoproteins PLZF, PLZF-RARalpha, and BCL-6. Wong CW, Privalsky ML. J. Biol. Chem. 273, 27695-702, (1998). View articlePMID: 9765306

10.Insights into SCF ubiquitin ligases from the structure of the Skp1-Skp2 complex. Schulman BA, Carrano AC, Jeffrey PD, Bowen Z, Kinnucan ER, Finnin MS, Elledge SJ, Harper JW, Pagano M, Pavletich NP. Nature 408, 381-6, (2000). View articlePMID: 11099048

Cross References

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