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Search results 101 to 124 out of 124 for Fnip2

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0.044s

Type

Details

Score

Publication

23582324 | J:201276

First Author:	Betschinger J
Year:	2013
Journal:	Cell
Title:	Exit from pluripotency is gated by intracellular redistribution of the bHLH transcription factor Tfe3.
Volume:	153
Issue:	2
Pages:	335-47

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Protein Domain

IPR026156 | FNIP_fam

Type:

Family

Description:

Birt-Hogg-Dube' syndrome, a disorder characterised by benign tumours of the hair follicle, lung cysts and renal neoplasia, is caused by germline mutations in the BHD(FLCN) gene; this encodes a tumour suppressor protein, folliculin (FLCN), of unknown function []. The folliculin- interacting protein, FNIP1, has also been identified and shown to interact with 5' AMP-activated protein kinase (AMPK), which plays a vital role in energy sensing []. Together, then, it is thought that folliculin (mutated in Birt-Hogg-Dube' syndrome) and its interaction partner, FNIP1, may be involved in energy and/or nutrient sensing via the AMPK and mTOR signalling pathways.FNIP1 has a homologue, FNIP2, which also interacts with FLCN and AMPK. C-terminally-deleted FLCN mutants, like those produced by germline mutations in BHD patients, do not bind FNIP2, suggesting that FLCN tumour-suppressor function may be facilitated by interactions with both FNIP1 and FNIP2 via its C terminus []. FNIP1 and FNIP2 are able to form homo- or heteromeric multimers, and may hence function either independently or cooperatively with FLCN [].This entry represents the FNIP family, including FNIP1 and FNIP2.

•

Protein Domain

IPR044886 | FLCN_DENN_C_sf

Type:

Homologous_superfamily

Description:

Folliculin (FLCN) is a tumor suppressor that enables nutrient-dependent activation of the mechanistic target of rapamycin complex 1 (mTORC1) protein kinase via its guanosine triphosphatase (GTPase) Activating Protein (GAP) activity. It belong to the DENN module family of proteins and contains a divergent DENN module comprised of a N-terminal longin domain (also known as upstream DENN domain, u-DENN), followed by a DENN domain. It forms a complex with its partners, FNIP1 or FNIP2 (Folliculin interacting protein 1 or 2), which directly contacts the Rag GTPases RagC/D to stimulate GTP hydrolysis and thus promote the conversion to the GDP-bound state. FLCN-FNIP2 adopts an extended conformation with two pairs of heterodimerized domains. They contain longin domains that heterodimerize and contact both nucleotide binding domains of the Rag heterodimer, and C-terminal DENN domains which interact at the distal end of the structure [, , ].This is a subdomain found at the C terminus in the DENN domain of folliculin.

•

Publication

12606363 | J:83525

First Author:	Brown PR
Year:	2003
Journal:	Biol Reprod
Title:	A-kinase anchoring protein 4 binding proteins in the fibrous sheath of the sperm flagellum.
Volume:	68
Issue:	6
Pages:	2241-8

•

Publication

27617292 | J:236977

First Author:	Yang M
Year:	2016
Journal:	Sci Adv
Title:	A C9ORF72/SMCR8-containing complex regulates ULK1 and plays a dual role in autophagy.
Volume:	2
Issue:	9
Pages:	e1601167

•

Publication

27559131 | -

First Author:	Amick J
Year:	2016
Journal:	Mol Biol Cell
Title:	C9orf72 binds SMCR8, localizes to lysosomes, and regulates mTORC1 signaling.
Volume:	27
Issue:	20
Pages:	3040-3051

•

Protein Domain

IPR032035 | Folliculin_DENN

Type:

Domain

Description:

Folliculin (FLCN) is a tumor suppressor that enables nutrient-dependent activation of the mechanistic target of rapamycin complex 1 (mTORC1) protein kinase via its guanosine triphosphatase (GTPase) Activating Protein (GAP) activity. It belong to the DENN module family of proteins and contains a divergent DENN module comprised of a N-terminal longin domain (also known as upstream DENN domain, u-DENN), followed by a DENN domain. It forms a complex with its partners, FNIP1 or FNIP2 (Folliculin interacting protein 1 or 2), which directly contacts the Rag GTPases RagC/D to stimulate GTP hydrolysis and thus promote the conversion to the GDP-bound state. FLCN-FNIP2 adopts an extended conformation with two pairs of heterodimerized domains. They contain longin domains that heterodimerize and contact both nucleotide binding domains of the Rag heterodimer, and C-terminal DENN domains which interact at the distal end of the structure [, , ].This is the DENN domain found at the C-terminal of folliculin. This domain shares structural similarity with DENN domain of DENN1B (a Rab GEF). It mediates contact with the longin domain in the heterodimers to ensure a strong intersubunit interaction [, , ].

•

Protein Domain

IPR037520 | Folliculin/SMCR8_longin

Type:

Domain

Description:

Folliculin (FLCN) is a tumor suppressor that enables nutrient-dependent activation of the mechanistic target of rapamycin complex 1 (mTORC1) protein kinase via its guanosine triphosphatase (GTPase) Activating Protein (GAP) activity. It belong to the DENN module family of proteins and contains a divergent DENN module comprised of a N-terminal longin domain (also known as upstream DENN domain, u-DENN), followed by a DENN domain. It forms a complex with its partners, FNIP1 or FNIP2 (Folliculin interacting protein 1 or 2), which directly contacts the Rag GTPases RagC/D to stimulate GTP hydrolysis and thus promote the conversion to the GDP-bound state. FLCN-FNIP2 adopts an extended conformation with two pairs of heterodimerized domains. They contain longin domains that heterodimerize and contact both nucleotide binding domains of the Rag heterodimer, and C-terminal DENN domains which interact at the distal end of the structure [, , ].This is the N-terminal domain of folliculin, the longin domain [, , ]. An arginine residue located in this domain (Arg164) is catalytic residue for GAP activity [, ]. This domain can also be found in SMCR8, a component of the C9orf72-SMCR8 complex, a complex that has guanine nucleotide exchange factor (GEF) activity and regulates autophagy [, , , , , ].

•

Protein

Q68FD7

Organism:	Mus musculus/domesticus
Length:	1165
Fragment?:	false

•

Protein

Q80TD3

Organism:	Mus musculus/domesticus
Length:	1108
Fragment?:	false

•

Protein

F6RJ64

Organism:	Mus musculus/domesticus
Length:	631
Fragment?:	true

•

Protein

D3YUC5

Organism:	Mus musculus/domesticus
Length:	1138
Fragment?:	false

•

Protein

A0A668KLU2

Organism:	Mus musculus/domesticus
Length:	677
Fragment?:	true

•

Publication

20562859 | -

First Author:	Behrends C
Year:	2010
Journal:	Nature
Title:	Network organization of the human autophagy system.
Volume:	466
Issue:	7302
Pages:	68-76

•

Protein

Q8QZS3

Organism:	Mus musculus/domesticus
Length:	579
Fragment?:	false

•

Publication

31704029 | -

First Author:	Shen K
Year:	2019
Journal:	Cell
Title:	Cryo-EM Structure of the Human FLCN-FNIP2-Rag-Ragulator Complex.
Volume:	179
Issue:	6
Pages:	1319-1329.e8

•

Publication

31672913 | -

First Author:	Lawrence RE
Year:	2019
Journal:	Science
Title:	Structural mechanism of a Rag GTPase activation checkpoint by the lysosomal folliculin complex.
Volume:	366
Issue:	6468
Pages:	971-977

•

Publication

27193190 | J:240578

First Author:	Sullivan PM
Year:	2016
Journal:	Acta Neuropathol Commun
Title:	The ALS/FTLD associated protein C9orf72 associates with SMCR8 and WDR41 to regulate the autophagy-lysosome pathway.
Volume:	4
Issue:	1
Pages:	51

•

Publication

28195531 | -

First Author:	Jung J
Year:	2017
Journal:	Elife
Title:	Multiplex image-based autophagy RNAi screening identifies SMCR8 as ULK1 kinase activity and gene expression regulator.
Volume:	6

•

Publication

23248642 | -

First Author:	Zhang D
Year:	2012
Journal:	Front Genet
Title:	Discovery of Novel DENN Proteins: Implications for the Evolution of Eukaryotic Intracellular Membrane Structures and Human Disease.
Volume:	3

Pages:	283

•

Protein

Q3UMB5

Organism:	Mus musculus/domesticus
Length:	935
Fragment?:	false

•

Publication

27103069 | J:233688

First Author:	Sellier C
Year:	2016
Journal:	EMBO J
Title:	Loss of C9ORF72 impairs autophagy and synergizes with polyQ Ataxin-2 to induce motor neuron dysfunction and cell death.
Volume:	35
Issue:	12
Pages:	1276-97

•

Publication

22977732 | -

First Author:	Nookala RK
Year:	2012
Journal:	Open Biol
Title:	Crystal structure of folliculin reveals a hidDENN function in genetically inherited renal cancer.
Volume:	2
Issue:	8
Pages:	120071

•

Publication

15489334 | -

First Author:	Gerhard DS
Year:	2004
Journal:	Genome Res
Title:	The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
Volume:	14
Issue:	10B
Pages:	2121-7

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