Regulated Intramembrane Proteolysis: Signaling Pathways and Biological Functions

Lal, Mark; Caplan, Michael J.

doi:10.1152/physiol.00028.2010

Cited by 90 publications

(87 citation statements)

References 74 publications

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“…Last, the reader is referred to other recent reviews on this topic Borlido et al 2009;McCarthy et al 2009;De Strooper and Annaert 2010;Ló pez-Otin and Hunter 2010;Wang et al 2010c;Lal and Caplan 2011;Lemberg 2011). …”

Section: Discussionmentioning

confidence: 99%

Receptor Tyrosine Kinases in the Nucleus

Carpenter

Liao

2013

Cold Spring Harbor Perspectives in Biology

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To date, 18 distinct receptor tyrosine kinases (RTKs) are reported to be trafficked from the cell surface to the nucleus in response to ligand binding or heterologous agonist exposure. In most cases, an intracellular domain (ICD) fragment of the receptor is generated at the cell surface and translocated to the nucleus, whereas for a few others the intact receptor is translocated to the nucleus. ICD fragments are generated by several mechanisms, including proteolysis, internal translation initiation, and messenger RNA (mRNA) splicing. The most prevalent mechanism is intramembrane cleavage by g-secretase. In some cases, more than one mechanism has been reported for the nuclear localization of a specific RTK. The generation and use of RTK ICD fragments to directly communicate with the nucleus and influence gene expression parallels the production of ICD fragments by a number of non-RTK cell-surface molecules that also influence cell proliferation. This review will be focused on the individual RTKs and to a lesser extent on other growth-related cell-surface transmembrane proteins.

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Section: Discussionmentioning

confidence: 99%

Receptor Tyrosine Kinases in the Nucleus

Carpenter

Liao

2013

Cold Spring Harbor Perspectives in Biology

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“…[33][34][35] RIP acts by a family of iCLiPs proteases that recognize the specific motifs and cleave the target protein within the hydrophobic environment of the membrane. HOPS belongs in a growing list of proteins that, in response to appropriate stimuli, release an activated intermediate isoform from the longer intramembrane isoform.…”

Section: Discussionmentioning

confidence: 99%

Different functions of HOPS isoforms in the cell

Castelli¹,

Piobbico

Bartoli³

et al. 2013

Cell Cycle

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“…The Jmj domain, present in a family of histone demethylases, 25 is also associated with low t 1/2 values. Some additional groups of proteins not shown in Figure 9 have very short half-lives, including (1) proteins documented to be modified by regulated intramembrane proteolysis (9.661.8 hours), 26 viz. Sdc1, Sorl1, Cdh1, Epcam, Lrp1, Lrp2, Itm2b, and App; and (2) transcription factors (25.661.3 hours) (Supplemental Dataset 4).…”

Section: Subpopulations Of Proteins With Short or Long Halflivesmentioning

confidence: 99%

Proteome-Wide Measurement of Protein Half-Lives and Translation Rates in Vasopressin-Sensitive Collecting Duct Cells

Sandoval

Slentz

Pisitkun

et al. 2013

Journal of the American Society of Nephrology

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Vasopressin regulates water excretion, in part, by controlling the abundances of the water channel aquaporin-2 (AQP2) protein and regulatory proteins in the renal collecting duct. To determine whether vasopressin-induced alterations in protein abundance result from modulation of protein production, protein degradation, or both, we used protein mass spectrometry with dynamic stable isotope labeling in cell culture to achieve a proteome-wide determination of protein half-lives and relative translation rates in mpkCCD cells. Measurements were made at steady state in the absence or presence of the vasopressin analog, desmopressin (dDAVP). Desmopressin altered the translation rate rather than the stability of most responding proteins, but it significantly increased both the translation rate and the half-life of AQP2. In addition, proteins associated with vasopressin action, including Mal2, Akap12, gelsolin, myosin light chain kinase, annexin-2, and Hsp70, manifested altered translation rates. Interestingly, desmopressin increased the translation of seven glutathione S-transferase proteins and enhanced protein S-glutathionylation, uncovering a previously unexplored vasopressin-induced post-translational modification. Additional bioinformatic analysis of the mpkCCD proteome indicated a correlation between protein function and protein half-life. In particular, processes that are rapidly regulated, such as transcription, endocytosis, cell cycle regulation, and ubiquitylation are associated with proteins with especially short half-lives. These data extend our understanding of the mechanisms underlying vasopressin signaling and provide a broad resource for additional investigation of collecting duct function (http://helixweb.nih.gov/ESBL/Database/ ProteinHalfLives/index.html). 24: 179324: -180524: , 201324: . doi: 10.1681 Vasopressin controls water excretion by regulating the molecular water channel aquaporin-2 (AQP2) in two fundamental ways: (1) regulated trafficking, 1 seen in a time frame of 40 seconds to about 40 minutes, 2 and (2) regulation of AQP2 protein abundance, typically seen after many hours of exposure to vasopressin. 3,4 Studies in animal models of various water balance disorders have revealed that most clinically important water balance abnormalities are associated with dysregulation of AQP2 abundance rather than trafficking. 5 High levels of circulating vasopressin for periods of hours to days in animals are associated with increases in AQP2 mRNA in the kidney. 6,7 Such observations have led to the widely accepted view that vasopressin regulates AQP2 abundance by transcriptional mechanisms. [8][9][10][11] However, recent studies in cultured inner medullary collecting duct (IMCD) cells by Nedvetsky et al. 12 have shown J Am Soc Nephrol

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Regulated Intramembrane Proteolysis: Signaling Pathways and Biological Functions

Cited by 90 publications

References 74 publications

Receptor Tyrosine Kinases in the Nucleus

Receptor Tyrosine Kinases in the Nucleus

Different functions of HOPS isoforms in the cell

Proteome-Wide Measurement of Protein Half-Lives and Translation Rates in Vasopressin-Sensitive Collecting Duct Cells

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