NDLI: R.I.P. to the PIP: PCNA-binding motif no longer considered specific

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R.I.P. to the PIP: PCNA-binding motif no longer considered specific

Content Provider	Scilit
Author	Boehm, Elizabeth M. Washington, M. Todd
Copyright Year	2016
Description	Journal: BioEssays Many proteins responsible for genome maintenance interact with one another via short sequence motifs. The best known of these are PIP motifs, which mediate interactions with the replication protein PCNA. Others include RIR motifs, which bind the translesion synthesis protein Rev1, and MIP motifs, which bind the mismatch repair protein Mlh1. Although these motifs have similar consensus sequences, they have traditionally been viewed as separate motifs, each with their own target protein. In this article, we review several recent studies that challenge this view. Taken together, they imply that these different motifs are not distinct entities. Instead, there is a single, broader class of motifs, which we call "PIP-like" motifs, which have overlapping specificities and are capable of binding multiple target proteins. Given this, we must reassess the role of these motifs in forming the network of interacting proteins responsible for genome maintenance.
Related Links	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5341575/pdf
Ending Page	1122
Page Count	6
Starting Page	1117
e-ISSN	15211878
DOI	10.1002/bies.201600116
Journal	BioEssays
Issue Number	11
Volume Number	38
Language	English
Publisher	Wiley-Blackwell
Publisher Date	2016-08-19
Access Restriction	Open
Subject Keyword	Journal: BioEssays Biochemistry and Molecular Biology Cell Biology Dna Recombination Dna Repair Dna Replication Translesion Synthesis
Content Type	Text
Resource Type	Article

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The Proliferating Cell Nuclear Antigen (PCNA)-interacting Protein (PIP) Motif of DNA Polymerase η Mediates Its Interaction with the C-terminal Domain of Rev1

The Proliferating Cell Nuclear Antigen (PCNA)-interacting Protein (PIP) Motif of DNA Polymerase η Mediates Its Interaction with the C-terminal Domain of Rev1

The ubiquitin-binding domain of DNA polymerase η directly binds to DNA clamp PCNA and regulates translesion DNA synthesis.

Identification of Small Molecule Proliferating Cell Nuclear Antigen (PCNA) Inhibitor That Disrupts Interactions with PIP-box Proteins and Inhibits DNA Replication

Proliferating Cell Nuclear Antigen (PCNA)-binding Protein C1orf124 Is a Regulator of Translesion Synthesis

A genetic study based on PCNA-ubiquitin fusions reveals no requirement for PCNA polyubiquitylation in DNA damage tolerance

Non-canonical binding of the Chaetomium thermophilum PolD4 N-terminal PIP motif to PCNA involves Q-pocket and compact 2-fork plug interactions but no 3₁₀ helix.

Role of Y-family translesion DNA polymerases in replication stress: Implications for new cancer therapeutic targets

Proliferating Cell Nuclear Antigen Promotes Translesion Synthesis by DNA Polymerase ζ

R.I.P. to the PIP: PCNA-binding motif no longer considered specific

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The Proliferating Cell Nuclear Antigen (PCNA)-interacting Protein (PIP) Motif of DNA Polymerase η Mediates Its Interaction with the C-terminal Domain of Rev1

The Proliferating Cell Nuclear Antigen (PCNA)-interacting Protein (PIP) Motif of DNA Polymerase η Mediates Its Interaction with the C-terminal Domain of Rev1

The ubiquitin-binding domain of DNA polymerase η directly binds to DNA clamp PCNA and regulates translesion DNA synthesis.

Identification of Small Molecule Proliferating Cell Nuclear Antigen (PCNA) Inhibitor That Disrupts Interactions with PIP-box Proteins and Inhibits DNA Replication

Proliferating Cell Nuclear Antigen (PCNA)-binding Protein C1orf124 Is a Regulator of Translesion Synthesis

A genetic study based on PCNA-ubiquitin fusions reveals no requirement for PCNA polyubiquitylation in DNA damage tolerance

Non-canonical binding of the Chaetomium thermophilum PolD4 N-terminal PIP motif to PCNA involves Q-pocket and compact 2-fork plug interactions but no 310 helix.

Role of Y-family translesion DNA polymerases in replication stress: Implications for new cancer therapeutic targets

Proliferating Cell Nuclear Antigen Promotes Translesion Synthesis by DNA Polymerase ζ

R.I.P. to the PIP: PCNA-binding motif no longer considered specific

Non-canonical binding of the Chaetomium thermophilum PolD4 N-terminal PIP motif to PCNA involves Q-pocket and compact 2-fork plug interactions but no 3₁₀ helix.