The PITP family of phosphatidylinositol transfer proteins

The PITP family is one of the two families of phosphoinositide transfer proteins that can bind and exchange one molecule of either phosphatidylinositol or phosphatidylcholine and facilitate the transfer of these lipids between different membrane compartments; the other is the structurally unrelated Sec14p family. PITPs have recently been shown to be critical regulators of phosphoinositides in several cellular compartments, where they participate in signal transduction and in membrane traffic. PITPs were originally defined as soluble, 35 kDa proteins that contain a single structural domain. More recently, however, the PITP domain has also been found in the larger rdgB proteins. Soluble PITPs are found in many organisms, including mammals, Caenorhabditis elegans (worms), Drosophila melanogaster (flies), and Dictyostelium discoideum (slime molds), but not in yeasts or plants. Dysfunction of PITPs leads to neurodegeneration; this highlights the need to understand the biochemical and physiological functions of these proteins in cells.

• Publication year

  2001

• Venue

  Genome Biology

• Publication date

  2001-08-31

• Fields of study

  Biology, Medicine

• Identifiers
  DOI 10.1186/gb-2001-2-9-reviews3011PMID 11574064PMCID 138965
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

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  2001cited by this paper
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  2001cited by this paper
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  2000influential reference
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  2000cited by this paper
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  2000cited by this paper
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  1999cited by this paper
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  1999influential reference
• Identification of a Novel Family of Targets of PYK2 Related to Drosophila Retinal Degeneration B (rdgB) Protein

  1999cited by this paper
• Involvement of PITPnm, a Mammalian Homologue of Drosophila rdgB, in Phosphoinositide Synthesis on Golgi Membranes*

  1999cited by this paper
• Cloning and Characterization of a Novel Human Phosphatidylinositol Transfer Protein, rdgBβ*

  1999cited by this paper
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  1999cited by this paper
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  1998cited by this paper
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  1998cited by this paper
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  1997cited by this paper
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  1997cited by this paper
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  1997cited by this paper
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  1997cited by this paper
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  1997cited by this paper
• The Phosphatidylinositol Transfer Protein Domain of Drosophila Retinal Degeneration B Protein Is Essential for Photoreceptor Cell Survival and Recovery from Light Stimulation

  1997cited by this paper
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  1997cited by this paper
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  1996cited by this paper
• τ Is Widely Expressed in Rat Tissues

  1996cited by this paper
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  1996cited by this paper
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  1996cited by this paper
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  1995cited by this paper
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  1995cited by this paper
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  1995cited by this paper
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  1995cited by this paper
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  1995cited by this paper
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  1994cited by this paper
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  1994cited by this paper
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  1993cited by this paper
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  1993cited by this paper
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  1993cited by this paper
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• Cigarette Smoke Extract Combined with LPS Upregulates PITPβ Expression in Chronic Pulmonary Inflammation and May Be Related to the EGFR/ERK Signaling Pathway.

  2026cites this paper
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  2026cites this paper
• Regulation of the MDM2-p53 Nexus by a Nuclear Phosphoinositide and Small Heat Shock Protein Complex

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  2025influential citation
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  2024cites this paper
• Structural organization of RDGB (retinal degeneration B), a multi-domain lipid transfer protein: a molecular modelling and simulation based approach

  2023cites this paper
• Role of SEC14-like phosphatidylinositol transfer proteins in membrane identity and dynamics

  2023cites this paper
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  2023cites this paper
• Ribosomal targeting strategy and nuclear labeling to analyze photoreceptor phosphoinositide signatures.

  2022cites this paper
• pitpβ_w Encoding Phosphatidylinositol Transfer Protein Is Involved in Female Differentiation of Chinese Tongue Sole, Cynoglossus semilaevis

  2022cites this paper
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  2022cites this paper
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  2021cites this paper
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  2021cites this paper
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  2021influential citation
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  2021cites this paper
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  2021cites this paper
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  2020cites this paper
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  2019cites this paper
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  2019cites this paper
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  2019cites this paper
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  2018cites this paper
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  2012cites this paper
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  2012cites this paper
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  2011cites this paper
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  2011cites this paper
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  2010cites this paper
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  2010cites this paper
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  2009cites this paper
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  2007cites this paper
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  2007cites this paper
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  2007cites this paper
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  2006cites this paper
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  2006cites this paper
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  2006cites this paper
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  2005cites this paper
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  2005cites this paper
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  2005cites this paper
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• Phosphatidylinositol transfer protein beta displays minimal sphingomyelin transfer activity and is not required for biosynthesis and trafficking of sphingomyelin.

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• Current thoughts on the phosphatidylinositol transfer protein family

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