Phosphoinositides Differentially Regulate Protrudin Localization through the FYVE Domain

Gil, Jung Eun; Kim, Eui; Kim, Il Shin; Ku, Bonsu; Park, Wei Sun; Oh, Byung Ha; Ryu, Sung Ho; Cho, Wonhwa; Heo, Won Do

doi:10.1074/jbc.m112.419127

Cited by 36 publications

(43 citation statements)

References 52 publications

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“…However, Saita et al (16) identified an interaction of protrudin with the ER-localized VAP-A, and Gil et al (17) localized some protrudin at ER, which increased dramatically upon deletion of the FYVE domain. Matsuzaki et al (25) used mass spectrometry to identify proteins interacting with protrudin, and a number were ER proteins, as well as the KIF5 molecular motor.…”

Section: Discussionmentioning

confidence: 99%

“…The FYVE domain is of particular interest because it mediates interactions with the plasma membrane (17), which might play a role in ER-network formation. We generated a mutant lacking the FYVE domain, and whereas protrusions were induced by overexpression of wild-type HA-protrudin, as described previously (13), expression of HA-tagged ΔFYVE protrudin did not induce these (Fig.…”

Section: Significancementioning

confidence: 99%

“…Depletion of VAP-A causes mislocalization of protrudin and inhibition of neurite outgrowth induced by nerve growth factor in PC12 cells (16). Protrudin proteins with FYVE domain mutations causing reduced phosphoinositide-binding affinity fail to promote neurite outgrowth in cultured neurons (17).…”

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confidence: 99%

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Protrudin binds atlastins and endoplasmic reticulum-shaping proteins and regulates network formation

Chang

Lee

Blackstone

2013

Proc. Natl. Acad. Sci. U.S.A.

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Hereditary spastic paraplegias are inherited neurological disorders characterized by progressive lower-limb spasticity and weakness. Although more than 50 genetic loci are known [spastic gait (SPG)1 to -57], over half of hereditary spastic paraplegia cases are caused by pathogenic mutations in four genes encoding proteins that function in tubular endoplasmic reticulum (ER) network formation: atlastin-1 (SPG3A), spastin (SPG4), reticulon 2 (SPG12), and receptor expression-enhancing protein 1 (SPG31). Here, we show that the SPG33 protein protrudin contains hydrophobic, intramembrane hairpin domains, interacts with tubular ER proteins, and functions in ER morphogenesis by regulating the sheet-to-tubule balance and possibly the density of tubule interconnections. Protrudin also interacts with KIF5 and harbors a Rab-binding domain, a noncanonical FYVE (Fab-1, YGL023, Vps27, and EEA1) domain, and a two phenylalanines in an acidic tract (FFAT) domain and, thus, may also function in the distribution of ER tubules via ER contacts with the plasma membrane or other organelles.

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Section: Discussionmentioning

confidence: 99%

Section: Significancementioning

confidence: 99%

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Protrudin binds atlastins and endoplasmic reticulum-shaping proteins and regulates network formation

Chang

Lee

Blackstone

2013

Proc. Natl. Acad. Sci. U.S.A.

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“…Interestingly, it has recently been shown for the neuronal protein protrudin, that its FYVE domain binds to other phospholipids including PI(4,5)P2 (Gil et al, 2012). It is possible that newly synthesized MOBP could also associate with PI(4,5)P2-containing lipid rafts.…”

Section: Fyn-mediated Translation Of Mobp Mrnamentioning

confidence: 99%

MOBP levels are regulated by Fyn kinase and affect the morphological differentiation of oligodendrocytes

Schäfer

Müller

Luhmann

et al. 2016

Journal of Cell Science

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Oligodendrocytes are the myelinating glial cells of the central nervous system (CNS). Myelin is formed by extensive wrapping of oligodendroglial processes around axonal segments, which ultimately allows a rapid saltatory conduction of action potentials within the CNS and sustains neuronal health. The non-receptor tyrosine kinase Fyn is an important signaling molecule in oligodendrocytes. It controls the morphological differentiation of oligodendrocytes and is an integrator of axon-glial signaling cascades leading to localized synthesis of myelin basic protein (MBP), which is essential for myelin formation. The abundant myelinassociated oligodendrocytic basic protein (MOBP) resembles MBP in several aspects and has also been reported to be localized as mRNA and translated in the peripheral myelin compartment. The signals initiating local MOBP synthesis are so far unknown and the cellular function of MOBP remains elusive. Here, we show, by several approaches in cultured primary oligodendrocytes, that MOBP synthesis is stimulated by Fyn activity. Moreover, we reveal a new function for MOBP in oligodendroglial morphological differentiation.

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“…These domains are highly homologous, and most FYVE domains specifically bind PI(3)P (Lemmon 2008; Kutateladze 2007; Kutateladze 2010)), although recently the FYVE domain of protrudin was shown to bind PI(4,5)P 2 , PI(3,4)P 2 , and PI(3,4,5,)P 3 (Gil et al 2012). Three motifs found in FYVE domains (WxxD, RR/KHHCR, and RVC) shape a cationic patch that interacts with PI(3)P. PI(3)P plays a key role in membrane trafficking and is found in specific subcellular locales, including the cytoplasmic face of early endosomes, multivesicular bodies, and phagosomes (Burd and Emr 1998; Gaullier et al 1998; Patki V et al 1998).…”

Section: Phosphoinositide Binding Modulesmentioning

confidence: 99%

Cellular and molecular interactions of phosphoinositides and peripheral proteins

Stahelin

Scott

Frick

2014

Chemistry and Physics of Lipids

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Anionic lipids act as signals for the recruitment of proteins containing cationic clusters to biological membranes. A family of anionic lipids known as the phosphoinositides (PIPs) are low in abundance, yet play a critical role in recruitment of peripheral proteins to the membrane interface. PIPs are mono-, bis-, or trisphosphorylated derivatives of phosphatidylinositol (PI) yielding seven species with different structure and anionic charge. The differential spatial distribution and temporal appearance of PIPs is key to their role in communicating information to target proteins. Selective recognition of PIPs came into play with the discovery that the substrate of protein kinase C termed pleckstrin possessed the first PIP binding region termed the pleckstrin homology (PH) domain. Since the discovery of the PH domain, more than ten PIP binding domains have been identified including PH, ENTH, FYVE, PX, and C2 domains. Representative examples of each of these domains have been thoroughly characterized to understand how they coordinate PIP headgroups in membranes, translocate to specific membrane docking sites in the cell, and function to regulate the activity of their full-length proteins. In addition, a number of novel mechanisms of PIP-mediated membrane association have emerged, such as coincidence detection – specificity for two distinct lipid headgroups. Other PIP-binding domains may also harbor selectivity for a membrane physical property such as charge or membrane curvature. This review summarizes the current understanding of the cellular distribution of PIPs and their molecular interaction with peripheral proteins.

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Phosphoinositides Differentially Regulate Protrudin Localization through the FYVE Domain

Cited by 36 publications

References 52 publications

Protrudin binds atlastins and endoplasmic reticulum-shaping proteins and regulates network formation

Protrudin binds atlastins and endoplasmic reticulum-shaping proteins and regulates network formation

MOBP levels are regulated by Fyn kinase and affect the morphological differentiation of oligodendrocytes

Cellular and molecular interactions of phosphoinositides and peripheral proteins

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