INT274602

Context Info Confidence 0.17 First Reported 2009 Last Reported 2009 Negated 0 Speculated 0 Reported most in Body Documents 1 Total Number 7 Disease Relevance 0.25 Pain Relevance 0.07

endoplasmic reticulum (BFAR) structural molecule activity (BFAR)

Anatomy Link Frequency filaments 2 BFAR (Homo sapiens)

Pain Link Frequency Relevance Heat Inflammation 63 84.24 Pain 14 5.00 Arthritis 14 5.00

Disease Link Frequency Relevance Heat INFLAMMATION 63 84.24 Disease 70 55.44 Syndrome 63 53.52 Fever 77 46.56 Osteomyelitis 28 30.72 Pain 14 5.00 Arthritis 14 5.00 Acne 14 5.00 Pyoderma Gangrenosum 14 5.00 Adhesions 7 5.00

Sentences Mentioned In

Key:

Protein

Mutation

Event

Anatomy

Negation

Speculation

Pain term

Disease term

In the presence of full length PSTPIP1, the protein containing only the F-BAR domain (FCH-X-CC) is able to bind to formed filaments, but the uncharacterized “Y” region between the coiled coil and the SH3 domain appears to be additionally required for the generation of filaments (Figure 2).

BAR Binding (bind) of in filaments

1) Confidence 0.17 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2702820 Disease Relevance 0.11 Pain Relevance 0.03

The F-BAR region, encompassing the FCH and the CC, was able bind to filaments formed by full-length PSTPIP1 (Figure 2B–D).

BAR Binding (bind) of in filaments

2) Confidence 0.13 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2702820 Disease Relevance 0 Pain Relevance 0

Indeed, the homologous F-BAR domain of CIP4 interacts with microtubules [14] and the related N-BAR family member, amphiphysin, interacts with a linker protein (CLIP-170) that binds to microtubules [29].

BAR Binding (binds) of

3) Confidence 0.13 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2702820 Disease Relevance 0 Pain Relevance 0

Indeed, the homologous F-BAR domain of CIP4 interacts with microtubules [14] and the related N-BAR family member, amphiphysin, interacts with a linker protein (CLIP-170) that binds to microtubules [29].

BAR Binding (binds) of

4) Confidence 0.13 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2702820 Disease Relevance 0 Pain Relevance 0

Taken together, these data confirm that PSTPIP1 shares the lipid membrane-binding properties of several other F-BAR domain-containing proteins, a property that is not affected by pyrin binding.

BAR Binding (binding) of

5) Confidence 0.13 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2702820 Disease Relevance 0.06 Pain Relevance 0

Indeed, the F-BAR domains of both PSTPIP1 and PSTPIP2 can bind to artificial liposomes containing phosphatidyl inositol (4,5) bisphosphate (PI(4,5)P2) with high affinity [19].

BAR Binding (bind) of

6) Confidence 0.12 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2702820 Disease Relevance 0 Pain Relevance 0

It will be important to determine whether PSTPIP1 binds directly to microtubules, like the related F-BAR protein, CIP4 [14], or whether the interaction is via an intermediate microtubule binding protein, as in the case of amphiphysin [29].

F-BAR protein Binding (binds) of

7) Confidence 0.11 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2702820 Disease Relevance 0.08 Pain Relevance 0.04

General Comments

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